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and the ideal choice depends on their area of application. A dataset together with implementations of a number of popular models (HMM, CRF) for activity recognition can be found here. Conventional temporal probabilistic models such as the hidden Markov model (HMM) and conditional random fields (CRF) model directly model the correlations between the activities and the observed sensor data. In recent years, increasing evidence has supported the use of hierarchical models which take into account the rich hierarchical structure that exists in human behavioral data. The core idea here is that the model does not directly correlate the activities with the sensor data, but instead breaks the activity into sub-activities (sometimes referred to as actions) and models the underlying correlations accordingly. An example could be the activity of preparing a stir fry, which can be broken down into the subactivities or actions of cutting vegetables, frying the vegetables in a pan and serving it on a plate. Examples of such a hierarchical model are Layered Hidden Markov Models (LHMMs) and the hierarchical hidden Markov model (HHMM), which have been shown to significantly outperform its non-hierarchical counterpart in activity recognition. === Data mining based approach to activity recognition === Different from traditional machine learning approaches, an approach based on data mining has been recently proposed. In the work of Gu et al., the problem of activity recognition is formulated as a pattern-based classification problem. They proposed a data mining approach based on discriminative patterns which describe significant changes between any two activity classes of data to recognize sequential, interleaved and concurrent activities in a unified solution. Gilbert et al. use 2D corners in both space and time. These are grouped spatially and temporally using a hierarchical process, with an increasing search area. At each stage of the hierarchy, the most distinctive
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"page_id": 15795950,
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and descriptive features are learned efficiently through data mining (Apriori rule). === GPS-based activity recognition === Location-based activity recognition can also rely on GPS data to recognize activities. == Sensor usage == === Vision-based activity recognition === It is a very important and challenging problem to track and understand the behavior of agents through videos taken by various cameras. The primary technique employed is Computer Vision. Vision-based activity recognition has found many applications such as human-computer interaction, user interface design, robot learning, and surveillance, among others. Scientific conferences where vision based activity recognition work often appears are ICCV and CVPR. In vision-based activity recognition, a great deal of work has been done. Researchers have attempted a number of methods such as optical flow, Kalman filtering, Hidden Markov models, etc., under different modalities such as single camera, stereo, and infrared. In addition, researchers have considered multiple aspects on this topic, including single pedestrian tracking, group tracking, and detecting dropped objects. Recently some researchers have used RGBD cameras like Microsoft Kinect to detect human activities. Depth cameras add extra dimension i.e. depth which normal 2d camera fails to provide. Sensory information from these depth cameras have been used to generate real-time skeleton model of humans with different body positions. This skeleton information provides meaningful information that researchers have used to model human activities which are trained and later used to recognize unknown activities. With the recent emergency of deep learning, RGB video based activity recognition has seen rapid development. It uses videos captured by RGB cameras as input and perform several tasks, including: video classification, detection of activity start and end in videos, and spatial-temporal localization of activity and the people performing the activity. Pose estimation methods allow extracting more representative skeletal features for action recognition. That said, it has been discovered
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"page_id": 15795950,
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that deep learning based action recognition may suffer from adversarial attacks, where an attacker alter the input insignificantly to fool an action recognition system. Despite remarkable progress of vision-based activity recognition, its usage for most actual visual surveillance applications remains a distant aspiration. Conversely, the human brain seems to have perfected the ability to recognize human actions. This capability relies not only on acquired knowledge, but also on the aptitude of extracting information relevant to a given context and logical reasoning. Based on this observation, it has been proposed to enhance vision-based activity recognition systems by integrating commonsense reasoning and, contextual and commonsense knowledge. Hierarchical Human Activity (HAR) Recognition Hierarchical human activity recognition is a technique within computer vision and machine learning. It aims to identify and comprehend human actions or behaviors from visual data. This method entails structuring activities hierarchically, creating a framework that represents connections and interdependencies among various actions. HAR techniques can be used to understand data correlations and model fundamentals to improve models, to balance accuracy and privacy concerns in sensitive application areas, and to identify and manage trivial labels that have no relevance in specific use cases. ==== Levels of vision-based activity recognition ==== In vision-based activity recognition, the computational process is often divided into four steps, namely human detection, human tracking, human activity recognition and then a high-level activity evaluation. ==== Fine-grained action localization ==== In computer vision-based activity recognition, fine-grained action localization typically provides per-image segmentation masks delineating the human object and its action category (e.g., Segment-Tube). Techniques such as dynamic Markov Networks, CNN and LSTM are often employed to exploit the semantic correlations between consecutive video frames. Geometric fine-grained features such as objective bounding boxes and human poses facilitate activity recognition with graph neural network. ==== Automatic gait recognition ==== One way
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to identify specific people is by how they walk. Gait-recognition software can be used to record a person's gait or gait feature profile in a database for the purpose of recognizing that person later, even if they are wearing a disguise. === Wi-Fi-based activity recognition === When activity recognition is performed indoors and in cities using the widely available Wi-Fi signals and 802.11 access points, there is much noise and uncertainty. These uncertainties can be modeled using a dynamic Bayesian network model. In a multiple goal model that can reason about user's interleaving goals, a deterministic state transition model is applied. Another possible method models the concurrent and interleaving activities in a probabilistic approach. A user action discovery model could segment Wi-Fi signals to produce possible actions. ==== Basic models of Wi-Fi recognition ==== One of the primary thought of Wi-Fi activity recognition is that when the signal goes through the human body during transmission; which causes reflection, diffraction, and scattering. Researchers can get information from these signals to analyze the activity of the human body. ===== Static transmission model ===== As shown in, when wireless signals are transmitted indoors, obstacles such as walls, the ground, and the human body cause various effects such as reflection, scattering, diffraction, and diffraction. Therefore, receiving end receives multiple signals from different paths at the same time, because surfaces reflect the signal during the transmission, which is known as multipath effect. The static model is based on these two kinds of signals: the direct signal and the reflected signal. Because there is no obstacle in the direct path, direct signal transmission can be modeled by Friis transmission equation: P r = P t G t G r λ 2 ( 4 π ) 2 d 2 {\displaystyle P_{r}={\frac {P_{t}G_{t}G_{r}\lambda ^{2}}{(4\pi )^{2}d^{2}}}} P t {\displaystyle
|
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P_{t}} is the power fed into the transmitting antenna input terminals; P r {\displaystyle P_{r}} is the power available at receiving antenna output terminals; d {\displaystyle d} is the distance between antennas; G t {\displaystyle G_{t}} is transmitting antenna gain; G r {\displaystyle G_{r}} is receiving antenna gain; λ {\displaystyle \lambda } is the wavelength of the radio frequency If we consider the reflected signal, the new equation is: P r = P t G t G r λ 2 ( 4 π ) 2 ( d + 4 h ) 2 {\displaystyle P_{r}={\frac {P_{t}G_{t}G_{r}\lambda ^{2}}{(4\pi )^{2}(d+4h)^{2}}}} h {\displaystyle h} is the distance between reflection points and direct path. When human shows up, we have a new transmission path. Therefore, the final equation is: P r = P t G t G r λ 2 ( 4 π ) 2 ( d + 4 h + Δ ) 2 {\displaystyle P_{r}={\frac {P_{t}G_{t}G_{r}\lambda ^{2}}{(4\pi )^{2}(d+4h+\Delta )^{2}}}} Δ {\displaystyle \Delta } is the approximate difference of the path caused by human body. ===== Dynamic transmission model ===== In this model, we consider the human motion, which causes the signal transmission path to change continuously. We can use Doppler Shift to describe this effect, which is related to the motion speed. Δ f = 2 v cos θ c f {\displaystyle \Delta f={\frac {2v\cos \theta }{c}}f} By calculating the Doppler Shift of the receiving signal, we can figure out the pattern of the movement, thereby further identifying human activity. For example, in, the Doppler shift is used as a fingerprint to achieve high-precision identification for nine different movement patterns. ===== Fresnel zone ===== The Fresnel zone was initially used to study the interference and diffraction of the light, which is later used to construct the wireless signal transmission model. Fresnel zone is
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a series of elliptical intervals whose foci are the positions of the sender and receiver. When a person is moving across different Fresnel zones, the signal path formed by the reflection of the human body changes, and if people move vertically through Fresnel zones, the change of signal will be periodic. In a pair of papers, Wang et.al. applied the Fresnel model to the activity recognition task and got a more accurate result. ===== Modeling of the human body ===== In some tasks, we should consider modeling the human body accurately to achieve better results. For example, described the human body as concentric cylinders for breath detection. The outside of the cylinder denotes the rib cage when people inhale, and the inside denotes that when people exhale. So the difference between the radius of that two cylinders represents the moving distance during breathing. The change of the signal phases can be expressed in the following equation: θ = 2 π 2 Δ d λ {\displaystyle \theta =2\pi {\frac {2\,\Delta d}{\lambda }}} θ {\displaystyle \theta } is the change of the signal phases; λ {\displaystyle \lambda } is the wavelength of the radio frequency; Δ d {\displaystyle \Delta d} is moving distance of rib cage; == Datasets == There are some popular datasets that are used for benchmarking activity recognition or action recognition algorithms. UCF-101: It consists of 101 human action classes, over 13k clips and 27 hours of video data. Action classes include applying makeup, playing dhol, cricket shot, shaving beard, etc. HMDB51: This is a collection of realistic videos from various sources, including movies and web videos. The dataset is composed of 6,849 video clips from 51 action categories (such as “jump”, “kiss” and “laugh”), with each category containing at least 101 clips. Kinetics: This is a significantly larger
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dataset than the previous ones. It contains 400 human action classes, with at least 400 video clips for each action. Each clip lasts around 10s and is taken from a different YouTube video. This dataset was created by DeepMind. == Applications == By automatically monitoring human activities, home-based rehabilitation can be provided for people suffering from traumatic brain injuries. One can find applications ranging from security-related applications and logistics support to location-based services. Activity recognition systems have been developed for wildlife observation and energy conservation in buildings. == See also == AI effect Applications of artificial intelligence Conditional random field Gesture recognition Hidden Markov model Motion analysis Naive Bayes classifier Support vector machines Object co-segmentation Outline of artificial intelligence Video content analysis == References ==
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Americium oxide may refer to: Americium dioxide Americium(III) oxide == See also == Americium(III) hydroxide
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"page_id": 23463663,
"source": null,
"title": "Americium oxide"
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Fauna (pl.: faunae or faunas) is all of the animal life present in a particular region or time. The corresponding terms for plants and fungi are flora and funga, respectively. Flora, fauna, funga and other forms of life are collectively referred to as biota. Zoologists and paleontologists use fauna to refer to a typical collection of animals found in a specific time or place, e.g. the "Sonoran Desert fauna" or the "Burgess Shale fauna". Paleontologists sometimes refer to a sequence of faunal stages, which is a series of rocks all containing similar fossils. The study of animals of a particular region is called faunistics. == Etymology == Fauna comes from the name Fauna, a Roman goddess of earth and fertility, the Roman god Faunus, and the related forest spirits called Fauns. All three words are cognates of the name of the Greek god Pan, and panis is the Modern Greek equivalent of fauna (πανίς or rather πανίδα). Fauna is also the word for a book that catalogues the animals in such a manner. The term was first used by Carl Linnaeus from Sweden in the title of his 1745 work Fauna Suecica. == Subdivisions on the basis of region == === Cryofauna === Cryofauna refers to the animals that live in, or very close to, cold areas. === Cryptofauna === Cryptofauna is the fauna that exists in protected or concealed microhabitats. === Epifauna === Epifauna, also called epibenthos, are aquatic animals that live on the bottom substratum as opposed to within it, that is, the benthic fauna that live on top of the sediment surface at the seafloor. === Infauna === Infauna are benthic organisms that live within the bottom substratum of a water body, especially within the bottom-most oceanic sediments, the layer of small particles at the bottom of
|
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a body of water, rather than on its surface. Bacteria and microalgae may also live in the interstices of bottom sediments. In general, infaunal animals become progressively smaller and less abundant with increasing water depth and distance from shore, whereas bacteria show more constancy in abundance, tending toward one million cells per milliliter of interstitial seawater. Such creatures are found in the fossil record and include lingulata, trilobites and worms. They made burrows in the sediment as protection and may also have fed upon detritus or the mat of microbes which tended to grow on the surface of the sediment. Today, a variety of organisms live in and disturb the sediment. The deepest burrowers are the ghost shrimps (Thalassinidea), which go as deep as 3 metres (10 ft) into the sediment at the bottom of the ocean. === Limnofauna === Limnofauna refers to the animals that live in fresh water. === Macrofauna === Macrofauna are benthic or soil organisms which are retained on a 0.5 mm sieve. Studies in the deep sea define macrofauna as animals retained on a 0.3 mm sieve to account for the small size of many of the taxa. === Megafauna === Megafauna are large animals of any particular region or time. For example, Australian megafauna. === Meiofauna === Meiofauna are small benthic invertebrates that live in both marine and freshwater environments. The term meiofauna loosely defines a group of organisms by their size, larger than microfauna but smaller than macrofauna, rather than a taxonomic grouping. One environment for meiofauna is between grains of damp sand (see Mystacocarida). In practice these are metazoan animals that can pass unharmed through a 0.5–1 mm mesh but will be retained by a 30–45 μm mesh, but the exact dimensions will vary from researcher to researcher. Whether an organism passes
|
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through a 1 mm mesh also depends upon whether it is alive or dead at the time of sorting. === Mesofauna === Mesofauna are macroscopic soil animals such as arthropods or nematodes. Mesofauna are extremely diverse; considering just the springtails (Collembola), as of 1998, approximately 6,500 species had been identified. === Microfauna === Microfauna are microscopic or very small animals (usually including protozoans and very small animals such as rotifers). To qualify as microfauna, an organism must exhibit animal-like characteristics, as opposed to microflora, which are more plant-like. === Stygofauna === Stygofauna is any fauna that lives in groundwater systems or aquifers, such as caves, fissures and vugs. Stygofauna and troglofauna are the two types of subterranean fauna (based on life-history). Both are associated with subterranean environments – stygofauna is associated with water, and troglofauna with caves and spaces above the water table. Stygofauna can live within freshwater aquifers and within the pore spaces of limestone, calcrete or laterite, whilst larger animals can be found in cave waters and wells. Stygofaunal animals, like troglofauna, are divided into three groups based on their life history - stygophiles, stygoxenes, and stygobites. === Troglofauna === Troglofauna are small cave-dwelling animals that have adapted to their dark surroundings. Troglofauna and stygofauna are the two types of subterranean fauna (based on life-history). Both are associated with subterranean environments – troglofauna is associated with caves and spaces above the water table and stygofauna with water. Troglofaunal species include spiders, insects, myriapods and others. Some troglofauna live permanently underground and cannot survive outside the cave environment. Troglofauna adaptations and characteristics include a heightened sense of hearing, touch and smell. Loss of under-used senses is apparent in the lack of pigmentation as well as eyesight in most troglofauna. Troglofauna insects may exhibit a lack of wings and longer
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appendages. === Xenofauna === Xenofauna, theoretically, are alien organisms that can be described as animal analogues. While no alien life forms, animal-like or otherwise, are known definitively, the concept of alien life remains a subject of great interest in fields like astronomy, astrobiology, biochemistry, evolutionary biology, science fiction, and philosophy. === Other === Other terms include avifauna, which means "bird fauna" and piscifauna (or ichthyofauna), which means "fish fauna". == Treatises == === Classic faunas === Linnaeus, Carolus. Fauna Suecica. 1746 == See also == == References == == External links == "Biodiversity of Collembola and their functional role in the ecosystem" (by Josef Rusek; September 1998)
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"page_id": 722672,
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This list contains a list of EC numbers for the sixth group, EC 6, ligases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. == EC 6.1: Forming Carbon-Oxygen Bonds == === EC 6.1.1: Ligases Forming Aminoacyl-tRNA and Related Compounds (Aminoacyl tRNA synthetase) === EC 6.1.1.1: tyrosine—tRNA ligase EC 6.1.1.2: tryptophan—tRNA ligase EC 6.1.1.3: threonine—tRNA ligase EC 6.1.1.4: leucine—tRNA ligase EC 6.1.1.5: isoleucine—tRNA ligase EC 6.1.1.6: lysine—tRNA ligase EC 6.1.1.7: alanine—tRNA ligase EC 6.1.1.8: Deleted EC 6.1.1.9: valine—tRNA ligase EC 6.1.1.10: methionine—tRNA ligase EC 6.1.1.11: serine—tRNA ligase EC 6.1.1.12: aspartate—tRNA ligase EC 6.1.1.13: D-alanine—poly(phosphoribitol) ligase EC 6.1.1.14: glycine—tRNA ligase EC 6.1.1.15: proline—tRNA ligase EC 6.1.1.16: cysteine—tRNA ligase EC 6.1.1.17: glutamate—tRNA ligase EC 6.1.1.18: glutamine—tRNA ligase EC 6.1.1.19: arginine—tRNA ligase EC 6.1.1.20: phenylalanine—tRNA ligase EC 6.1.1.21: histidine—tRNA ligase EC 6.1.1.22: asparagine—tRNA ligase EC 6.1.1.23: aspartate—tRNAAsn ligase EC 6.1.1.24: glutamate—tRNAGln ligase EC 6.1.1.25: The tRNAPyl is now known only to be charged with pyrrolysine (cf. EC 6.1.1.26) EC 6.1.1.26: pyrrolysine—tRNAPyl ligase EC 6.1.1.27: O-phospho-L-serine—tRNA ligase EC 6.1.1.28: proline/cysteine—tRNA ligase. Later published work having demonstrated that this was not a genuine enzyme, EC 6.1.1.28 was withdrawn at the public-review stage before being made official === EC 6.1.2: Acid—alcohol ligases (ester synthases) === EC 6.1.2.1: D-alanine—(R)-lactate ligase EC 6.1.2.2: nebramycin 5′ synthase * * No Wikipedia article === EC 6.1.3: Cyclo-ligases === EC 6.1.3.1: olefin β-lactone synthetase * * No Wikipedia article == EC 6.2: Forming Carbon-Sulfur Bonds == === EC 6.2.1: Acid-Thiol Ligases === EC 6.2.1.1: acetate—CoA ligase EC 6.2.1.2: medium-chain acyl-CoA ligase EC 6.2.1.3: long-chain-fatty-acid—CoA ligase EC 6.2.1.4: succinate—CoA ligase (GDP-forming) EC 6.2.1.5: succinate—CoA ligase (ADP-forming) EC 6.2.1.6: glutarate—CoA ligase EC 6.2.1.7:
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cholate—CoA ligase EC 6.2.1.8: oxalate—CoA ligase EC 6.2.1.9: malate—CoA ligase EC 6.2.1.10: carboxylic acid—CoA ligase (GDP-forming) EC 6.2.1.11: biotin—CoA ligase EC 6.2.1.12: 4-coumarate—CoA ligase EC 6.2.1.13: acetate—CoA ligase (ADP-forming) EC 6.2.1.14: 6-carboxyhexanoate—CoA ligase EC 6.2.1.15: arachidonate—CoA ligase EC 6.2.1.16: acetoacetate—CoA ligase EC 6.2.1.17: propionate—CoA ligase EC 6.2.1.18: citrate—CoA ligase EC 6.2.1.19: long-chain-fatty-acid—protein ligase EC 6.2.1.20: long-chain-fatty-acid—[acyl-carrier-protein] ligase EC 6.2.1.21: Activity covered by EC 6.2.1.30, phenylacetate—CoA ligase EC 6.2.1.22: [citrate (pro-3S)-lyase] ligase EC 6.2.1.23: dicarboxylate—CoA ligase EC 6.2.1.24: phytanate—CoA ligase EC 6.2.1.25: benzoate—CoA ligase EC 6.2.1.26: o-succinylbenzoate—CoA ligase EC 6.2.1.27: 4-hydroxybenzoate—CoA ligase EC 6.2.1.28: 3α,7α-dihydroxy-5β-cholestanate—CoA ligase EC 6.2.1.29: Deleted, identical to EC 6.2.1.7, cholate—CoA ligase EC 6.2.1.30: phenylacetate—CoA ligase EC 6.2.1.31: 2-furoate—CoA ligase EC 6.2.1.32: anthranilate—CoA ligase EC 6.2.1.33: 4-chlorobenzoate—CoA ligase EC 6.2.1.34: trans-feruloyl—CoA synthase EC 6.2.1.35: acetate—[acyl-carrier protein] ligase EC 6.2.1.36: 3-hydroxypropionyl-CoA synthase EC 6.2.1.37: 3-hydroxybenzoate—CoA ligase EC 6.2.1.38: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase EC 6.2.1.39: [butirosin acyl-carrier protein]—L-glutamate ligase EC 6.2.1.40: 4-hydroxybutyrate—CoA ligase (AMP-forming) * EC 6.2.1.41: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate—CoA ligase * EC 6.2.1.42: 3-oxocholest-4-en-26-oate—CoA ligase * EC 6.2.1.43: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase * EC 6.2.1.44: 3-(methylthio)propionyl—CoA ligase * EC 6.2.1.45: E1 ubiquitin-activating enzyme * EC 6.2.1.46: L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase * EC 6.2.1.47: medium-chain-fatty-acid—[acyl-carrier-protein] ligase * EC 6.2.1.48: carnitine—CoA ligase * EC 6.2.1.49: long-chain fatty acid adenylyltransferase FadD28 * EC 6.2.1.50: 4-hydroxybenzoate adenylyltransferase FadD22 * EC 6.2.1.51: 4-hydroxyphenylalkanoate adenylyltransferase FadD29 * EC 6.2.1.52: L-firefly luciferin—CoA ligase * EC 6.2.1.53: L-proline—[L-prolyl-carrier protein] ligase * EC 6.2.1.54: D-alanine—[D-alanyl-carrier protein] ligase * EC 6.2.1.55: E1 SAMP-activating enzyme * EC 6.2.1.56: 4-hydroxybutyrate—CoA ligase (ADP-forming) * EC 6.2.1.57: long-chain fatty acid adenylase/transferase FadD23 * EC 6.2.1.58: isophthalate—CoA ligase * EC 6.2.1.59: long-chain fatty acid adenylase/transferase FadD26 * EC 6.2.1.60: marinolic acid—CoA ligase * EC 6.2.1.61: salicylate—[aryl-carrier protein] ligase * EC 6.2.1.62: 3,4-dihydroxybenzoate—[aryl-carrier protein] ligase * EC 6.2.1.63: L-arginine—[L-arginyl-carrier protein] ligase * EC 6.2.1.64: E1 NEDD8-activating enzyme * EC 6.2.1.65: salicylate—CoA
|
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ligase * EC 6.2.1.66: glyine—[glycyl-carrier protein] ligase * EC 6.2.1.67: L-alanine—[L-alanyl-carrier protein] ligase * EC 6.2.1.68: L-glutamate—[L-glutamyl-carrier protein] ligase * EC 6.2.1.69: L-cysteine—[L-cysteinyl-carrier protein] ligase * EC 6.2.1.70: L-threonine—[L-threonyl-carrier protein] ligase * EC 6.2.1.71: 2,3-dihydroxybenzoate—[aryl-carrier protein] ligase * EC 6.2.1.72: L-serine—[L-seryl-carrier protein] ligase * EC 6.2.1.73: L-tryptophan—[L-tryptophyl-carrier protein] ligase * EC 6.2.1.74: 3-amino-5-hydroxybenzoate—[acyl-carrier protein] ligase * EC 6.2.1.75: indoleacetate—CoA ligase * EC 6.2.1.76: malonate—CoA ligase * * No Wikipedia article === EC 6.2.2: Amide—thiol ligases === EC 6.2.2.1: thioglycine synthase * EC 6.2.2.2: oxazoline synthase * EC 6.2.2.3: thiazoline synthase * * No Wikipedia article == EC 6.3: Forming Carbon-Nitrogen Bonds == === EC 6.3.1: Acid—Ammonia (or Amine) Ligases (Amide Synthases) === EC 6.3.1.1: aspartate—ammonia ligase EC 6.3.1.2: glutamine synthetase EC 6.3.1.3: Now EC 6.3.4.13, phosphoribosylamine—glycine ligase EC 6.3.1.4: aspartate—ammonia ligase (ADP-forming) EC 6.3.1.5: NAD+ synthase EC 6.3.1.6: glutamate—ethylamine ligase EC 6.3.1.7: 4-methyleneglutamate—ammonia ligase EC 6.3.1.8: glutathionylspermidine synthase EC 6.3.1.9: trypanothione synthase EC 6.3.1.10: adenosylcobinamide-phosphate synthase EC 6.3.1.11: glutamate—putrescine ligase EC 6.3.1.12: D-aspartate ligase EC 6.3.1.13: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranoside ligase EC 6.3.1.14: diphthine—ammonia ligase EC 6.3.1.15: 8-demethylnovobiocic acid synthase * EC 6.3.1.16: The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 6.3.3.6, carbapenam-3-carboxylate synthase EC 6.3.1.17: β-citrylglutamate synthase * EC 6.3.1.18: γ-glutamylanilide synthase * EC 6.3.1.19: prokaryotic ubiquitin-like protein ligase * EC 6.3.1.20: lipoate—protein ligase * EC 6.3.1.21: phosphoribosylglycinamide formyltransferase 2 * * No Wikipedia article === EC 6.3.2: Acid—Amino-Acid Ligases (Peptide Synthases) === EC 6.3.2.1: pantoate—β-alanine ligase (AMP-forming) EC 6.3.2.2: glutamate—cysteine ligase EC 6.3.2.3: glutathione synthase EC 6.3.2.4: D-alanine—D-alanine ligase EC 6.3.2.5: phosphopantothenate—cysteine ligase (CTP) EC 6.3.2.6: phosphoribosylaminoimidazolesuccinocarboxamide synthase EC 6.3.2.7: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase EC 6.3.2.8: UDP-N-acetylmuramate—L-alanine ligase EC 6.3.2.9: UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase EC 6.3.2.10: UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase EC 6.3.2.11: carnosine synthase EC 6.3.2.12: dihydrofolate synthase EC 6.3.2.13: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase EC 6.3.2.14: enterobactin synthase
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}
|
EC 6.3.2.15: Deleted, The activity observed is due to EC 6.3.2.10, UDP-N-acetylmuramoyl-tripeptideD-alanyl-D-alanine ligase EC 6.3.2.16: D-alanine—alanyl-poly(glycerolphosphate) ligase EC 6.3.2.17: tetrahydrofolate synthase EC 6.3.2.18: γ-glutamylhistamine synthase EC 6.3.2.19: The ubiquitinylation process is now known to be performed by several enzymes in sequence, starting with EC 6.2.1.45 (ubiquitin-activating enzyme E1) and followed by several transfer reactions, including those of EC 2.3.2.23 (E2 ubiquitin-conjugating enzyme) and EC 2.3.2.27 (RING-type E3 ubiquitin transferase) EC 6.3.2.20: indoleacetate—lysine synthetase EC 6.3.2.21: The reaction is performed by the sequential action of EC 6.2.1.45 (ubiquitin-activating enzyme E1), several ubiquitin transferases and finally by EC 2.3.2.27 [ubiquitin transferase RING E3 (calmodulin-selective)] EC 6.3.2.22: Now EC 6.3.1.14, diphthine—ammonia ligase. EC 6.3.2.23: homoglutathione synthase EC 6.3.2.24: tyrosine—arginine ligase EC 6.3.2.25: tubulin—tyrosine ligase EC 6.3.2.26: N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase EC 6.3.2.27: The activity is covered by two independent enzymes, EC 6.3.2.38 N2-citryl-N6-acetyl-N6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase EC 6.3.2.28: Now EC 6.3.2.49, L-alanine-L-anticapsin ligase EC 6.3.2.29: cyanophycin synthase (L-aspartate-adding) EC 6.3.2.30: cyanophycin synthase (L-arginine-adding) EC 6.3.2.31: coenzyme F420-0:L-glutamate ligase EC 6.3.2.32: coenzyme γ-F420-2:α-L-glutamate ligase EC 6.3.2.33: tetrahydrosarcinapterin synthase EC 6.3.2.34: coenzyme F420-0:L-glutamate ligase EC 6.3.2.35: D-alanine—D-serine ligase EC 6.3.2.36: 4-phosphopantoate—β-alanine ligase EC 6.3.2.37: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase EC 6.3.2.38: N2-citryl-N6-acetyl-N6-hydroxylysine synthase EC 6.3.2.39: aerobactin synthase EC 6.3.2.40: cyclopeptine synthase * EC 6.3.2.41: N-acetylaspartylglutamate synthase * EC 6.3.2.42: N-acetylaspartylglutamylglutamate synthase * EC 6.3.2.43: [amino-group carrier protein]—L-2-aminoadipate ligase * EC 6.3.2.44: pantoate—β-alanine ligase (ADP-forming) * EC 6.3.2.45: UDP-N-acetylmuramate—L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate ligase * EC 6.3.2.46: fumarate—(S)-2,3-diaminopropanoate ligase * EC 6.3.2.47: dapdiamide synthase * EC 6.3.2.48: L-arginine-specific L-amino acid ligase * EC 6.3.2.49: L-alanine—L-anticapsin ligase * EC 6.3.2.50: tenuazonic acid synthetase * EC 6.3.2.51: phosphopantothenate—cysteine ligase (ATP) * EC 6.3.2.52: jasmonoyl—L-amino acid ligase * EC 6.3.2.53: UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase * EC 6.3.2.54: L-2,3-diaminopropanoate—citrate ligase * EC 6.3.2.55: 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase * EC 6.3.2.56: staphyloferrin B synthase * EC 6.3.2.57: staphyloferrin A synthase *
|
{
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
}
|
EC 6.3.2.58: D-ornithine—citrate ligase * EC 6.3.2.59: 3-methyl-D-ornithine—L-lysine ligase * EC 6.3.2.60: glutamate—[amino group carrier protein] ligase * EC 6.3.2.61: tubulin-glutamate ligase * EC 6.3.2.62: β-tubulin-glutamate ligase * * No Wikipedia article === EC 6.3.3: Cyclo-Ligases === EC 6.3.3.1: phosphoribosylformylglycinamidine cyclo-ligase EC 6.3.3.2: 5-formyltetrahydrofolate cyclo-ligase EC 6.3.3.3: dethiobiotin synthase EC 6.3.3.4: (carboxyethyl)arginine β-lactam-synthase EC 6.3.3.5: O-ureido-D-serine cyclo-ligase * EC 6.3.3.6: carbapenam-3-carboxylate synthase * EC 6.3.3.7: Ni-sirohydrochlorin a,c-diamide reductive cyclase * * No Wikipedia article === EC 6.3.4: Other Carbon-Nitrogen Ligases === EC 6.3.4.1: Now included in EC 6.3.5.2, GMP synthase (glutamine-hydrolysing) EC 6.3.4.2: CTP synthase (glutamine hydrolysing) EC 6.3.4.3: formate—tetrahydrofolate ligase EC 6.3.4.4: adenylosuccinate synthase EC 6.3.4.5: argininosuccinate synthase EC 6.3.4.6: urea carboxylase EC 6.3.4.7: ribose-5-phosphate—ammonia ligase EC 6.3.4.8: imidazoleacetate—phosphoribosyldiphosphate ligase EC 6.3.4.9: biotin—[methylmalonyl-CoA-carboxytransferase] ligase EC 6.3.4.10: biotin—[methylmalonyl-CoA-carboxytransferase] ligase EC 6.3.4.11: biotin—[methylcrotonoyl-CoA-carboxylase] ligase EC 6.3.4.12: glutamate—methylamine ligase EC 6.3.4.13: phosphoribosylamine—glycine ligase EC 6.3.4.14: biotin carboxylase EC 6.3.4.15: biotin—[biotin carboxyl-carrier protein] ligase EC 6.3.4.16: carbamoyl-phosphate synthase (ammonia) EC 6.3.4.17: formate—dihydrofolate ligase EC 6.3.4.18: 5-(carboxyamino)imidazole ribonucleotide synthase EC 6.3.4.19: tRNAIle-lysidine synthase EC 6.3.4.20: 7-cyano-7-deazaguanine synthase EC 6.3.4.21: nicotinate phosphoribosyltransferase EC 6.3.4.22: tRNAIle2-agmatinylcytidine synthase * EC 6.3.4.23: formate—phosphoribosylaminoimidazolecarboxamide ligase * EC 6.3.4.24: tyramine—L-glutamate ligase * EC 6.3.4.25: 2-amino-2′-deoxyadenylo-succinate synthase * * No Wikipedia article === EC 6.3.5: Carbon-nitrogen ligases with glutamine as amido-N-donor === EC 6.3.5.1: NAD+ synthase (glutamine-hydrolysing) EC 6.3.5.2: GMP synthase (glutamine-hydrolysing) EC 6.3.5.3: phosphoribosylformylglycinamidine synthase EC 6.3.5.4: asparagine synthase (glutamine-hydrolysing) EC 6.3.5.5: carbamoyl-phosphate synthase (glutamine-hydrolysing) EC 6.3.5.6: asparaginyl-tRNA synthase (glutamine-hydrolysing) EC 6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolysing) EC 6.3.5.8: Now EC 2.6.1.85, aminodeoxychorismate synthase. As ATP is not hydrolysed during the reaction, the classification of the enzyme as a ligase was incorrect EC 6.3.5.9: hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) EC 6.3.5.10: adenosylcobyric acid synthase (glutamine-hydrolysing) EC 6.3.5.11: cobyrinate a,c-diamide synthase EC 6.3.5.12: Ni-sirohydrochlorin a,c-diamide synthase * EC 6.3.5.13: lipid II isoglutaminyl synthase
|
{
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
}
|
(glutamine-hydrolysing) * * No Wikipedia article == EC 6.4: Forming Carbon-Carbon Bonds == === EC 6.4.1: Ligases that form carbon-carbon bonds (only sub-subclass identified to date) === EC 6.4.1.1: pyruvate carboxylase EC 6.4.1.2: acetyl-CoA carboxylase EC 6.4.1.3: propionyl-CoA carboxylase EC 6.4.1.4: methylcrotonoyl-CoA carboxylase EC 6.4.1.5: geranoyl-CoA carboxylase EC 6.4.1.6: acetone carboxylase EC 6.4.1.7: 2-oxoglutarate carboxylase EC 6.4.1.8: acetophenone carboxylase EC 6.4.1.9: coenzyme F430 synthetase * *No Wikipedia article == EC 6.5: Forming Phosphoric Ester Bonds == === EC 6.5.1: Ligases that form phosphoric-ester bonds (only sub-subclass identified to date) === EC 6.5.1.1: DNA ligase (ATP) EC 6.5.1.2: DNA ligase (NAD+) EC 6.5.1.3: RNA ligase (ATP) EC 6.5.1.4: RNA 3′-terminal-phosphate cyclase (ATP) EC 6.5.1.5: RNA 3′-terminal-phosphate cyclase (GTP) * EC 6.5.1.6: DNA ligase (ATP or NAD+) * EC 6.5.1.7: DNA ligase (ATP, ADP or GTP) * EC 6.5.1.8: 3′-phosphate/5′-hydroxy nucleic acid ligase * EC 6.5.1.9: cyclic 2,3-diphosphoglycerate synthase * * No Wikipedia article == EC 6.6: Forming Nitrogen-Metal Bonds == === EC 6.6.1: Forming Coordination Complexes === EC 6.6.1.1: magnesium chelatase EC 6.6.1.2: cobaltochelatase == EC 6.7: Forming nitrogen-nitrogen bonds == === EC 6.7.1: Forming diazo bonds === EC 6.7.1.1: 3-amino-2-hydroxy-4-methoxybenzoate * * No Wikipedia article == References ==
|
{
"page_id": 5506803,
"source": null,
"title": "List of EC numbers (EC 6)"
}
|
Surface photovoltage (SPV) measurements are a widely used method to determine the minority carrier diffusion length of semiconductors. Since the transport of minority carriers determines the behavior of the p-n junctions that are ubiquitous in semiconductor devices, surface photovoltage data can be very helpful in understanding their performance. As a contactless method, SPV is a popular technique for characterizing poorly understood compound semiconductors where the fabrication of ohmic contacts or special device structures may be difficult. == Theory == As the name suggests, SPV measurements involve monitoring the potential of a semiconductor surface while generating electron-hole pairs with a light source. The surfaces of semiconductors are often depletion regions (or space charge regions) where a built-in electric field due to defects has swept out mobile charge carriers. A reduced carrier density means that the electronic energy band of the majority carriers is bent away from the Fermi level. This band-bending gives rise to a surface potential. When a light source creates electron-hole pairs deep within the semiconductor, they must diffuse through the bulk before reaching the surface depletion region. The photogenerated minority carriers have a shorter diffusion length than the much more numerous majority carriers, with which they can radiatively recombine. The change in surface potential upon illumination is therefore a measure of the ability of minority carriers to reach the surface, namely the minority carrier diffusion length. As always in diffusive processes, the diffusion length L {\displaystyle L} is approximately related to the lifetime τ b u l k {\displaystyle \tau _{\mathrm {bulk} }} by the expression L = D τ b u l k {\displaystyle L={\sqrt {D\tau _{\mathrm {bulk} }}}} , where D {\displaystyle D} is the diffusion coefficient. The diffusion length is independent of any built-in fields in contrast to the drift behavior of the carriers. Note
|
{
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
}
|
that the photogenerated majority carriers will also diffuse towards the surface but their number as a fraction of the thermally generated majority carrier density in a moderately doped semiconductor will be too small to create a measurable photovoltage. Both carrier types will also diffuse towards the rear contact where their collection can confuse interpretation of the data when the diffusion lengths are larger than the film thickness. In a real semiconductor, the measured diffusion length L m e a s = D τ e f f {\displaystyle L_{\mathrm {meas} }={\sqrt {D\tau _{\mathrm {eff} }}}} includes the effect of surface recombination, which is best understood through its effect on carrier lifetime: 1 τ e f f = 1 τ b u l k + 2 s d {\displaystyle {\frac {1}{\tau _{\mathrm {eff} }}}={\frac {1}{\tau _{\mathrm {bulk} }}}+{\frac {2s}{d}}} where τ e f f {\displaystyle \tau _{\mathrm {eff} }} is the effective carrier lifetime, τ b u l k {\displaystyle \tau _{\mathrm {bulk} }} is the bulk carrier lifetime, s {\displaystyle s} is the surface recombination velocity and d {\displaystyle d} is the film or wafer thickness. Even for well characterized materials, uncertainty about the value of the surface recombination velocity reduces the accuracy with which the diffusion length can be determined for thinner films. == Experimental methods == Surface photovoltage measurements are performed by placing a wafer or sheet film of a semiconducting material on a ground electrode and positioning a kelvin probe a small distance above the sample. The surface is illuminated with light of fixed wavelength in industrial applications or with light whose wavelength is scanned using a monochromator so as to vary the absorption depth of the photons. The deeper in the semiconductor that carrier generation occurs, the fewer the number of minority carriers that will reach the
|
{
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
}
|
surface and the smaller the photovoltage. On a semiconductor whose spectral absorption coefficient is known, the minority carrier diffusion length can in principle be extracted from a measurement of photovoltage versus wavelength. The optical properties of a novel semiconductor may not be well known or may not be homogeneous across the sample. The temperature of the semiconductor must be carefully controlled during an SPV measurement test thermal drift complicate the comparison of different samples. Typically SPV measurements are done in an AC-coupled fashion using a chopped light source rather than a vibrating Kelvin probe. == Significance == The minority carrier diffusion length is critical in determining the performance of devices such as photoconducting detectors and bipolar transistors. In both cases the ratio of the diffusion length to the device dimensions determines the gain. In photovoltaic devices, photodiodes and field-effect transistors, the drift behavior due to built-in fields is more important under typical conditions than the diffusive behavior. Even so the SPV is a convenient method of measuring the density of impurity-derived recombination centers that limit device performance. SPV is performed both as an automated and routine test of material quality in a production environment and as an experimental tool to probe the behavior of less well studied semiconducting materials. Time-resolved photoluminescence is an alternate contactless method of determining minority carrier transport properties. == See also == Kelvin probe force microscope Photo-reflectance Scanning Kelvin probe == References == Schroder, Dieter K. (2006). Semiconductor Material and Device Characterization. Wiley-IEEE Press. ISBN 978-0-471-73906-7. Schroder, Dieter K. (2001). "Surface voltage and surface photovoltage: history, theory and applications". Meas. Sci. Technol. 12 (3): R16 – R31. Bibcode:2001MeScT..12R..16S. doi:10.1088/0957-0233/12/3/202. Kronik, L.; Shapira, Y. (1999). "Surface photovoltage phenomena: theory, experiment, and applications" (PDF). Surface Science Reports. 37 (1): 1–206. Bibcode:1999SurSR..37....1K. CiteSeerX 10.1.1.471.8047. doi:10.1016/S0167-5729(99)00002-3. Archived from the original
|
{
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
}
|
(PDF) on 2005-03-12. Retrieved 2008-07-03. == External links == Freiberg Instruments vendor of industrial and scientific SPV and Minority Carrier Lifetime measurement systems Semilab vendor of commercial SPV and Minority Carrier Lifetime measurement systems KP Technology vendors of and consultants about Kelvin probes ASTM standard F391-96 "Standard Test Methods for Minority Carrier Diffusion Length in Extrinsic Semiconductors by Measurement of Steady-State Surface Photovoltage"
|
{
"page_id": 7800566,
"source": null,
"title": "Surface photovoltage"
}
|
The molecular formula C12H12N4O3 (molar mass: 260.25 g/mol, exact mass: 260.0909 u) may refer to: Benznidazole Furafylline
|
{
"page_id": 32376569,
"source": null,
"title": "C12H12N4O3"
}
|
Post-acute infection syndromes (PAISs) or post-infectious syndromes are medical conditions characterized by symptoms attributed to a prior infection. While it is commonly assumed that people either recover or die from infections, long-term symptoms—or sequelae—are a possible outcome as well. Examples include long COVID (post-acute sequelae of SARS-CoV-2 infection, PASC), Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS), and post-Ebola virus syndrome. Common symptoms include post-exertional malaise (PEM), severe fatigue, neurocognitive symptoms, flu-like symptoms, and pain. The pathology of most of these conditions is not understood and management is generally symptomatic. == Symptoms and signs == PAIS symptoms are often non-specific and similar despite diverse prior infections. Symptoms commonly included in definitions of PAIS include post-exertional malaise, severe fatigue, neurocognitive and sensory symptoms, flu-like symptoms, unrefreshing sleep, muscle pain, and joint pain. Symptoms can vary among affected people. Some PAIS symptoms are more specific. For example, eye problems are common in post-Ebola virus syndrome, and profound weakness is seen in post-polio syndrome and post-West Nile fevers. Symptoms can be severe and debilitating, resulting in lowered quality of life or inability to work. The onset of symptoms may be delayed, often by decades in the case of post-polio syndrome, and their severity may fluctuate over time. == Causes == Pathogens associated with PAISs include SARS-CoV-2 (causing COVID-19), Ebolavirus, Dengue virus, poliovirus, SARS-CoV-1 (causing SARS), Chikungunya virus, Epstein–Barr virus (EBV), West Nile virus (WNV), Ross River virus (RRV), Coxsackie B, influenza A virus subtype H1N1, varicella zoster virus (VZV), Coxiella burnetii, Borrelia, and Giardia. However, the strength of evidence associating these pathogens with chronic illness varies. The pathophysiology of most PAISs is poorly understood, but the overlap in symptoms despite disparate infectious triggers implies a possible shared pathology. For most conditions, no chronic infection has been detected. == Mechanism == The pathology of post-acute infections syndromes
|
{
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
}
|
is not understood. The commonality in symptoms between illnesses may point to a common pathology. Major hypotheses include persistence of the original pathogen or its remnants, autoimmunity, chronic inflammation, reactivation of other latent infections, microbiome dysbiosis, or damage to organs, which may include the lungs, brain, kidneys, heart, or blood vessels. == Diagnosis == In the absence of tests for most PAISes, diagnosis is usually based on the patient's history, symptoms, and eliminating other potential causes. Available tests often fail to explain patients' symptoms, but this does not suggest they are not real. The complexity of diagnosing PAISes may lead to long delays in diagnosis. Diagnostic criteria vary among illnesses, and have at times been the subject of intense debate. For example, several definitions of ME/CFS have been in use. === Classification === PAIS is a broad term describing conditions attributed to various infections, including long COVID, ME/CFS, post-Ebola virus syndrome, post-dengue fatigue syndrome, post-polio syndrome, post-SARS syndrome, post-chikungunya disease, Q fever fatigue syndrome, post-treatment Lyme disease syndrome (PTLDS), and symptoms observed after other infections lacking a specific name. Other known sequelae of infections include multisystem inflammatory syndrome in children (MIS-C), and subacute sclerosing panencephalitis (a deadly consequence of measles that can be delayed by years). == Management == Treatment options for most PAISes are limited. In general, the focus is on managing symptoms, and management strategies for ME/CFS may benefit patients with similar symptoms. == Prognosis == Some people with PAISs recover over a period ranging from weeks to years while others remain ill. Many studies have shown that symptoms can continue for at least several years until the studies' conclusion. Studies of PTLDS ran longer and found increased rates of symptoms for up to 27 years. In the case of ME/CFS prognosis is poor and the illness is
|
{
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
}
|
lifelong for most. == Epidemiology == Data on epidemiology is limited by the lack of large, rigorous studies; and rates vary by infection. Mononucleosis is among the best studied, and available studies found that 7-9% had persistent symptoms 12 months after infection, and 4% had serious symptoms after 2 years. The British Office of National Statistics data on long COVID say that about 10% of people who had COVID-19 self-reported long COVID 6 months after infection, and about 7% reported long COVID with activity limitations. An Australian study of EBV, C. burnetii, and Ross River Virus found that 11% of participants met the criteria for ME/CFS at 6 months. Around 10-20% of people with SARS also experienced long-term effects. == History == While PAISs were described prior to the COVID-19 pandemic, the emergence of long COVID brought them increased attention. == Society and culture == PAISs cause a significant disease burden, but have received relatively little attention from scientists, potentially delaying the discovery of causes, diagnostic tests, and treatments. Infectious disease surveillance programs track acute illness but rarely track the health effects of PAISes. Many doctors are also unfamiliar with them, and may fail to take symptoms seriously. == Research == PAISs may have a common cause, and different hypotheses are being studied. Long COVID has increased the overall pace of research. Yale School of Medicine operates a research center, founded in 2023, that focuses on PAISs called the Center for Infection & Immunity. == See also == Postural orthostatic tachycardia syndrome, sometimes attributed to an infection == References ==
|
{
"page_id": 74712827,
"source": null,
"title": "Post-acute infection syndrome"
}
|
Ljungström air preheater is an air preheater invented by the Swedish engineer Fredrik Ljungström (1875–1964). The patent was achieved in 1930. The factory and workshop were in Lidingö throughout the 1920s, with about 70 employees. In the 1930s, the facilities were used as a film studio, and they were demolished in the 1970s to give space for new development. In 1995, the Ljungström air preheater was distinguished as the 185th International Historic Mechanical Engineering Landmark by the American Society of Mechanical Engineers. Ljungström's technology of the air preheater is implemented in a vast number of modern power stations around the world, with total attributed worldwide fuel savings estimated at 4,960,000,000 tons of oil, "few inventions have been as successful in saving fuel as the Ljungström Air Preheater". In modern boilers, the preheater can provide up to 20% of the total heat transfer in the boiler process, while only representing 2% of the investment. == References == == External links == History of the Ljungström Air Preheater LJUNGSTRÖM Air Preheater (APH) & Gas-gas Heater (GGH) Power Plant Overview
|
{
"page_id": 53937915,
"source": null,
"title": "Ljungström air preheater"
}
|
C55-isoprenyl pyrophosphate (also known as undecaprenyl pyrophosphate or C55-PP) is an essential molecule involved in the construction of the bacterial peptidoglycan cell wall. It is a receptor found in the plasma membrane of bacteria allowing glycan tetrapeptide monomers synthesized in the cell cytoplasm to translocate to the periplasmic space. C55-P (undecaprenyl phosphate) is a related compound, containing one fewer phosphate group. It is produced from C55-PP by reaction EC 3.6.1.27, typically catalyzed by UppP/BacA. C55-P is recycled back into C55-PP later in the process. C55-OH is known as bactoprenol. == References ==
|
{
"page_id": 26478333,
"source": null,
"title": "C55-isoprenyl pyrophosphate"
}
|
Microbial population biology is the application of the principles of population biology to microorganisms. == Distinguishing from other biological disciplines == Microbial population biology, in practice, is the application of population ecology and population genetics toward understanding the ecology and evolution of bacteria, archaebacteria, microscopic fungi (such as yeasts), additional microscopic eukaryotes (e.g., "protozoa" and algae), and viruses. Microbial population biology also encompasses the evolution and ecology of community interactions (community ecology) between microorganisms, including microbial coevolution and predator-prey interactions. In addition, microbial population biology considers microbial interactions with more macroscopic organisms (e.g., host-parasite interactions), though strictly this should be more from the perspective of the microscopic rather than the macroscopic organism. A good deal of microbial population biology may be described also as microbial evolutionary ecology. On the other hand, typically microbial population biologists (unlike microbial ecologists) are less concerned with questions of the role of microorganisms in ecosystem ecology, which is the study of nutrient cycling and energy movement between biotic as well as abiotic components of ecosystems. Microbial population biology can include aspects of molecular evolution or phylogenetics. Strictly, however, these emphases should be employed toward understanding issues of microbial evolution and ecology rather than as a means of understanding more universal truths applicable to both microscopic and macroscopic organisms. The microorganisms in such endeavors consequently should be recognized as organisms rather than simply as molecular or evolutionary reductionist model systems. Thus, the study of RNA in vitro evolution is not microbial population biology and nor is the in silico generation of phylogenies of otherwise non-microbial sequences, even if aspects of either may in some (especially unintentional) manner be analogous to evolution in actual microbial populations. Microbial population biology can (and often does) involve the testing of more-general ecological and evolutionary hypotheses. Again, it is important to
|
{
"page_id": 7538436,
"source": null,
"title": "Microbial population biology"
}
|
retain some emphasis on the microbe since at some point this "question-driven" microbial population biology becomes instead population biology using microorganisms. Because the point of departure of these potentially disparate emphases can be somewhat arbitrary, there exist vague and not universally accepted delimits around what the discipline of microbial population biology does and does not constitute. == Microbial Population Biology Gordon conference == A Microbial Population Biology Gordon Research Conference is held every odd year, to date in New England (and usually in New Hampshire). The 2007 conference web page introduces the meetings as: Microbial Population Biology covers a diverse range of cutting edge issues in the microbial sciences and beyond. Firmly founded in evolutionary biology and with a strongly integrative approach, past meetings have covered topics ranging from the dynamics and genetics of adaptation to the evolution of mutation rate, community ecology, evolutionary genomics, altruism, and epidemiology. This meeting is never dull: some of the most significant and contentious issues in biology have been thrashed out here. A history of the meeting can be found here. The next Microbial Population Biology Gordon conference is scheduled for 2025. Information on past (and future) meetings is summarized as follows: == See also == Microbial cooperation Microbial consortium Microbial food web Microbial intelligence Microbial loop == External links == Microbial Population Biology Phage meetings Human microbiome project
|
{
"page_id": 7538436,
"source": null,
"title": "Microbial population biology"
}
|
This list contains a list of EC numbers for the fifth group, EC 5, isomerases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. == EC 5.1: Epimerases and racemases == === EC 5.1.1: Acting on Amino acids and Derivatives === EC 5.1.1.1: alanine racemase EC 5.1.1.2: methionine racemase EC 5.1.1.3: glutamate racemase EC 5.1.1.4: proline racemase EC 5.1.1.5: lysine racemase EC 5.1.1.6: threonine racemase EC 5.1.1.7: diaminopimelate epimerase EC 5.1.1.8: 4-hydroxyproline epimerase EC 5.1.1.9: arginine racemase EC 5.1.1.10: amino-acid racemase EC 5.1.1.11: phenylalanine racemase (ATP-hydrolysing) EC 5.1.1.12: ornithine racemase EC 5.1.1.13: aspartate racemase EC 5.1.1.14: nocardicin-A epimerase EC 5.1.1.15: 2-aminohexano-6-lactam racemase EC 5.1.1.16: protein-serine epimerase EC 5.1.1.17: isopenicillin-N epimerase EC 5.1.1.18: serine racemase EC 5.1.1.20: L-Ala-D/L-Glu epimerase * EC 5.1.1.21: isoleucine 2-epimerase * EC 5.1.1.22: 4-hydroxyproline betaine 2-epimerase * EC 5.1.1.23: UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate epimerase * EC 5.1.1.24: histidine racemase * *No Wikipedia article === EC 5.1.2: Acting on Hydroxy acids and Derivatives === EC 5.1.2.1: lactate racemase EC 5.1.2.2: mandelate racemase EC 5.1.2.3: 3-hydroxybutyryl-CoA epimerase EC 5.1.2.4: acetoin racemase EC 5.1.2.5: tartrate epimerase EC 5.1.2.6: isocitrate epimerase EC 5.1.2.7: tagaturonate epimerase * *No Wikipedia article === EC 5.1.3: Acting on Carbohydrates and Derivatives === EC 5.1.3.1: ribulose-phosphate 3-epimerase EC 5.1.3.2: UDP-glucose 4-epimerase EC 5.1.3.3: aldose 1-epimerase EC 5.1.3.4: L-ribulose-5-phosphate 4-epimerase EC 5.1.3.5: UDP-arabinose 4-epimerase EC 5.1.3.6: UDP-glucuronate 4-epimerase EC 5.1.3.7: UDP-N-acetylglucosamine 4-epimerase EC 5.1.3.8: N-acylglucosamine 2-epimerase EC 5.1.3.9: N-acylglucosamine-6-phosphate 2-epimerase EC 5.1.3.10: CDP-paratose 2-epimerase EC 5.1.3.11: cellobiose epimerase EC 5.1.3.12: The enzyme has never been purified and the activity was later shown not to exist EC 5.1.3.13: dTDP-4-dehydrorhamnose 3,5-epimerase EC 5.1.3.14: UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) EC 5.1.3.15: glucose-6-phosphate 1-epimerase EC 5.1.3.16:
|
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UDP-glucosamine 4-epimerase EC 5.1.3.17: heparosan-N-sulfate-glucuronate 5-epimerase EC 5.1.3.18: GDP-mannose 3,5-epimerase EC 5.1.3.19: chondroitin-glucuronate 5-epimerase EC 5.1.3.20: ADP-glyceromanno-heptose 6-epimeras EC 5.1.3.21: maltose epimerase EC 5.1.3.22: L-ribulose-5-phosphate 3-epimerase EC 5.1.3.23: UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase EC 5.1.3.24: N-acetylneuraminate epimerase EC 5.1.3.25: dTDP-L-rhamnose 4-epimerase EC 5.1.3.26: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase * EC 5.1.3.27: dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase * EC 5.1.3.28: UDP-N-acetyl-L-fucosamine synthase * EC 5.1.3.29: L-fucose mutarotase * EC 5.1.3.30: D-psicose 3-epimerase * EC 5.1.3.31: D-tagatose 3-epimerase * EC 5.1.3.32: L-rhamnose mutarotase * EC 5.1.3.33: 2-epi-5-epi-valiolone epimerase * EC 5.1.3.34: monoglucosyldiacylglycerol epimerase * EC 5.1.3.35: 2-epi-5-epi-valiolone 7-phosphate 2-epimerase * EC 5.1.3.36: heparosan-glucuronate 5-epimerase * EC 5.1.3.37: mannuronan 5-epimerase * EC 5.1.3.38: D-erythrulose 1-phosphate 3-epimerase * EC 5.1.3.39: L-erythrulose 4-phosphate epimerase. The activity has been shown not to take place. * EC 5.1.3.40: D-tagatose 6-phosphate 4-epimerase * EC 5.1.3.41: fructoselysine 3-epimerase * EC 5.1.3.42: D-glucosamine-6-phosphate 4-epimerase * EC 5.1.3.43: sulfoquinovose mutarotase * EC 5.1.3.44: mannose 2-epimerase * *No Wikipedia article === EC 5.1.99: Acting on Other Compounds === EC 5.1.99.1: methylmalonyl-CoA epimerase EC 5.1.99.2: 16-hydroxysteroid epimerase EC 5.1.99.3: allantoin racemase EC 5.1.99.4: α-methylacyl-CoA racemase EC 5.1.99.5: hydantoin racemase EC 5.1.99.6: NAD(P)H-hydrate epimerase EC 5.1.99.7: dihydroneopterin triphosphate 2′-epimerase * EC 5.1.99.8: 7,8-dihydroneopterin epimerase * *No Wikipedia article == EC 5.2: cis-trans-Isomerases == === EC 5.2.1: cis-trans Isomerases (only sub-subclass identified to date) === EC 5.2.1.1: maleate isomerase EC 5.2.1.2: maleylacetoacetate isomerase EC 5.2.1.3: Now known to be catalysed by a pathway involving EC 1.1.1.300, NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase; and EC 1.1.1.315, 11-cis-retinol dehydrogenase. EC 5.2.1.4: maleylpyruvate isomerase EC 5.2.1.5: linoleate isomerase EC 5.2.1.6: furylfuramide isomerase EC 5.2.1.7: transferred to EC 3.1.1.64, retinoid isomerohydrolase EC 5.2.1.8: peptidylprolyl isomerase EC 5.2.1.9: farnesol 2-isomerase EC 5.2.1.10: 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase EC 5.2.1.11: The existence of this enzyme has been called into question by one of the authors of the reference
|
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cited EC 5.2.1.12: ζ-carotene isomerase EC 5.2.1.13: prolycopene isomerase EC 5.2.1.14: β-carotene isomerase == EC 5.3: Intramolecular Oxidoreductases == === EC 5.3.1: Interconverting Aldoses and Ketoses === EC 5.3.1.1: triose-phosphate isomerase EC 5.3.1.2: deleted EC 5.3.1.3: D-arabinose isomerase EC 5.3.1.4: L-arabinose isomerase EC 5.3.1.5: xylose isomerase EC 5.3.1.6: ribose-5-phosphate isomerase EC 5.3.1.7: mannose isomerase EC 5.3.1.8: mannose-6-phosphate isomerase EC 5.3.1.9: glucose-6-phosphate isomerase EC 5.3.1.10: Now EC 3.5.99.6, glucosamine-6-phosphate deaminase EC 5.3.1.11: deleted EC 5.3.1.12: glucuronate isomerase EC 5.3.1.13: arabinose-5-phosphate isomerase EC 5.3.1.14: L-rhamnose isomerase EC 5.3.1.15: D-lyxose ketol-isomerase EC 5.3.1.16: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase EC 5.3.1.17: 5-dehydro-4-deoxy-D-glucuronate isomerase EC 5.3.1.18: deleted: reaction is due to EC 5.3.1.9 glucose-6-phosphate isomerase, in the presence of arsenate, or EC 5.3.1.5 xylose isomerase EC 5.3.1.19: Now EC 2.6.1.16, glutamine—fructose-6-phosphate transaminase (isomerizing) EC 5.3.1.20: ribose isomerase EC 5.3.1.21: corticosteroid side-chain-isomerase EC 5.3.1.22: hydroxypyruvate isomerase EC 5.3.1.23: S-methyl-5-thioribose-1-phosphate isomerase EC 5.3.1.24: phosphoribosylanthranilate isomerase EC 5.3.1.25: L-fucose isomerase EC 5.3.1.26: galactose-6-phosphate isomerase EC 5.3.1.27: 6-phospho-3-hexuloisomerase EC 5.3.1.28: D-sedoheptulose 7-phosphate isomerase EC 5.3.1.29: ribose 1,5-bisphosphate isomerase * EC 5.3.1.30: 5-deoxy-glucuronate isomerase * EC 5.3.1.31: sulfoquinovose isomerase * EC 5.3.1.32: (4S)-4-hydroxy-5-phosphooxypentane-2,3-dione isomerase * EC 5.3.1.33: L-erythrulose 1-phosphate isomerase * EC 5.3.1.34: D-erythrulose 4-phosphate isomerase * EC 5.3.1.35: 2-dehydrotetronate isomerase * EC 5.3.1.36: D-apiose isomerase * *No Wikipedia article === EC 5.3.2: Interconverting Keto- and Enol-Groups === EC 5.3.2.1: phenylpyruvate tautomerase EC 5.3.2.2: oxaloacetate tautomerase EC 5.3.2.3: TDP-4-oxo-6-deoxy-α-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-galactopyranose-forming) EC 5.3.2.4: TDP-4-oxo-6-deoxy-α-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-glucopyranose-forming) EC 5.3.2.5: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase EC 5.3.2.6: 2-hydroxymuconate tautomerase EC 5.3.2.7: ascopyrone tautomerase EC 5.3.2.8: 4-oxalomesaconate tautomerase === EC 5.3.3: Transposing C=C Bonds === EC 5.3.3.1: steroid Δ-isomerase EC 5.3.3.2: isopentenyl-diphosphate Δ-isomerase EC 5.3.3.3: vinylacetyl-CoA Δ-isomerase EC 5.3.3.4: muconolactone Δ-isomerase EC 5.3.3.5: cholestenol Δ-isomerase EC 5.3.3.6: methylitaconate Δ-isomerase EC 5.3.3.7: aconitate Δ-isomerase EC 5.3.3.8: Δ3-Δ2-enoyl-CoA isomerase EC 5.3.3.9: prostaglandin-A1 Δ-isomerase EC 5.3.3.10: 5-carboxymethyl-2-hydroxymuconate Δ-isomerase EC 5.3.3.11: isopiperitenone Δ-isomerase EC 5.3.3.12:
|
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L-dopachrome isomerase EC 5.3.3.13: polyenoic fatty acid isomerase EC 5.3.3.14: trans-2-decenoyl-[acyl-carrier protein] isomerase EC 5.3.3.15: Now EC 5.3.2.7, ascopyrone tautomerase EC 5.3.3.16: Now EC 5.3.2.8, 4-oxalomesaconate tautomerase EC 5.3.3.17: trans-2,3-dihydro-3-hydroxyanthranilate isomerase EC 5.3.3.18: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase EC 5.3.3.19: 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase * EC 5.3.3.20: Now EC 5.4.99.64, 2-hydroxyisobutanoyl-CoA mutase EC 5.3.3.21: Δ3,5-Δ2,4-dienoyl-CoA isomerase * EC 5.3.3.22: lutein isomerase * EC 5.3.3.23: S-methyl-5-thioribulose 1-phosphate isomerase * *No Wikipedia article === EC 5.3.4: Transposing S-S Bonds === EC 5.3.4.1: protein disulfide-isomerase === EC 5.3.99: Other Intramolecular Oxidoreductases === EC 5.3.99.1: deleted, reaction due to combined action of EC 4.2.1.92 (hydroperoxide dehydratase) and EC 5.3.99.6 (allene-oxide cyclase) EC 5.3.99.2: prostaglandin-D synthase EC 5.3.99.3: prostaglandin-E synthase EC 5.3.99.4: prostaglandin-I synthase EC 5.3.99.5: thromboxane-A synthase EC 5.3.99.6: allene-oxide cyclase EC 5.3.99.7: styrene-oxide isomerase EC 5.3.99.8: capsanthin/capsorubin synthase EC 5.3.99.9: neoxanthin synthase EC 5.3.99.10: thiazole tautomerase EC 5.3.99.11: 2-keto-myo-inositol isomerase * *No Wikipedia article == EC 5.4: Intramolecular Transferases == === EC 5.4.1: Transferring Acyl Groups === EC 5.4.1.1: lysolecithin acylmutase EC 5.4.1.2: Now EC 5.4.99.61, precorrin-8X methylmutase EC 5.4.1.3: 2-methylfumaryl-CoA isomerase * EC 5.4.1.4: D-galactarolactone isomerase * *No Wikipedia article === EC 5.4.2: Phosphotransferases (Phosphomutases) === EC 5.4.2.1: Now recognized as two separate enzymes EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and EC 5.4.2.12, phosphoglycerate mutase (2,3-diphosphoglycerate-independent) EC 5.4.2.2: phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent) EC 5.4.2.3: phosphoacetylglucosamine mutase EC 5.4.2.4: bisphosphoglycerate mutase EC 5.4.2.5: phosphoglucomutase (glucose-cofactor) EC 5.4.2.6: β-phosphoglucomutase EC 5.4.2.7: phosphopentomutase EC 5.4.2.8: phosphomannomutase EC 5.4.2.9: phosphoenolpyruvate mutase EC 5.4.2.10: phosphoglucosamine mutase EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) EC 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent) EC 5.4.2.13: phosphogalactosamine mutase * *No Wikipedia article === EC 5.4.3: Transferring Amino Groups === EC 5.4.3.1: deleted; this reaction was due to a mixture of EC 5.1.1.12 (ornithine racemase) and EC 5.4.3.5 (D-ornithine 4,5-aminomutase) EC 5.4.3.2: lysine 2,3-aminomutase EC 5.4.3.3: lysine 5,6-aminomutase EC 5.4.3.4: Now included in EC
|
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5.4.3.3, lysine 5,6-aminomutase EC 5.4.3.5: D-ornithine 4,5-aminomutase EC 5.4.3.6: tyrosine 2,3-aminomutase EC 5.4.3.7: leucine 2,3-aminomutase EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase EC 5.4.3.9: glutamate 2,3-aminomutase EC 5.4.3.10: phenylalanine aminomutase (L-β-phenylalanine forming) * EC 5.4.3.11: phenylalanine aminomutase (D-β-phenylalanine forming) * *No Wikipedia article === EC 5.4.4: Transferring hydroxy groups === EC 5.4.4.1: (hydroxyamino)benzene mutase EC 5.4.4.2: isochorismate synthase EC 5.4.4.3: 3-(hydroxyamino)phenol mutase EC 5.4.4.4: geraniol isomerase EC 5.4.4.5: 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase EC 5.4.4.6: 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase EC 5.4.4.7: hydroperoxy icosatetraenoate isomerase * EC 5.4.4.8: linalool isomerase * *No Wikipedia article === EC 5.4.99: Transferring Other Groups === EC 5.4.99.1: methylaspartate mutase EC 5.4.99.2: methylmalonyl-CoA mutase EC 5.4.99.3: 2-acetolactate mutase EC 5.4.99.4: 2-methyleneglutarate mutase EC 5.4.99.5: chorismate mutase EC 5.4.99.6: Now EC 5.4.4.2, isochorismate synthase EC 5.4.99.7: lanosterol synthase EC 5.4.99.8: cycloartenol synthase EC 5.4.99.9: UDP-galactopyranose mutase EC 5.4.99.10: Now included with EC 5.4.99.11, isomaltulose synthase EC 5.4.99.11: isomaltulose synthase EC 5.4.99.12: tRNA pseudouridine38-40 synthase EC 5.4.99.13: isobutyryl-CoA mutase EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase EC 5.4.99.15: (1→4)-α-D-glucan 1-α-D-glucosylmutase EC 5.4.99.16: maltose α-D-glucosyltransferase EC 5.4.99.17: squalene—hopene cyclase EC 5.4.99.18: 5-(carboxyamino)imidazole ribonucleotide mutase EC 5.4.99.19: 16S rRNA pseudouridine516 synthase EC 5.4.99.20: 23S rRNA pseudouridine2457 synthase EC 5.4.99.21: 23S rRNA pseudouridine2604 synthase EC 5.4.99.22: 23S rRNA pseudouridine2605 synthase EC 5.4.99.23: 23S rRNA pseudouridine1911/1915/1917 synthase EC 5.4.99.24: 23S rRNA pseudouridine955/2504/2580 synthase EC 5.4.99.25: tRNA pseudouridine55 synthase EC 5.4.99.26: tRNA pseudouridine65 synthase EC 5.4.99.27: tRNA pseudouridine13 synthase EC 5.4.99.28: RNA pseudouridine32 synthase EC 5.4.99.29: 23S rRNA pseudouridine746 synthase EC 5.4.99.30: UDP-arabinopyranose mutase EC 5.4.99.31: thalianol synthase EC 5.4.99.32: protostadienol synthase EC 5.4.99.33: cucurbitadienol synthase EC 5.4.99.34: germanicol synthase EC 5.4.99.35: taraxerol synthase EC 5.4.99.36: isomultiflorenol synthase EC 5.4.99.37: dammaradiene synthase EC 5.4.99.38: camelliol C synthase EC 5.4.99.39: β-amyrin synthase EC 5.4.99.40: α-amyrin synthase EC 5.4.99.41: lupeol synthase EC 5.4.99.42: tRNA pseudouridine31 synthase EC 5.4.99.43: 21S rRNA pseudouridine2819 synthase EC 5.4.99.44:
|
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"page_id": 5506829,
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"title": "List of EC numbers (EC 5)"
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mitochondrial tRNA pseudouridine27/28 synthase EC 5.4.99.45: tRNA pseudouridine38/39 synthase EC 5.4.99.46: shionone synthase EC 5.4.99.47: parkeol synthase EC 5.4.99.48: achilleol B synthase EC 5.4.99.49: glutinol synthase EC 5.4.99.50: friedelin synthase EC 5.4.99.51: baccharis oxide synthase EC 5.4.99.52: α-seco-amyrin synthase EC 5.4.99.53: marneral synthase EC 5.4.99.54: β-seco-amyrin synthase EC 5.4.99.55: δ-amyrin synthase EC 5.4.99.56: tirucalladienol synthase EC 5.4.99.57: baruol synthase EC 5.4.99.58: methylornithine synthase EC 5.4.99.59: dTDP-fucopyranose mutase * EC 5.4.99.60: cobalt-precorrin-8 methylmutase * EC 5.4.99.61: precorrin-8X methylmutase * EC 5.4.99.62: D-ribose pyranase * EC 5.4.99.63: ethylmalonyl-CoA mutase * EC 5.4.99.64: 2-hydroxyisobutanoyl-CoA mutase * EC 5.4.99.65: pre-α-onocerin synthase * EC 5.4.99.66: α-onocerin synthase * EC 5.4.99.67: 4-amino-4-deoxychorismate mutase * *No Wikipedia article == EC 5.5: Intramolecular Lyases == === EC 5.5.1: Intramolecular lyases (only sub-subclass identified to date) === EC 5.5.1.1: muconate cycloisomerase EC 5.5.1.2: 3-carboxy-cis,cis-muconate cycloisomerase EC 5.5.1.3: tetrahydroxypteridine cycloisomerase EC 5.5.1.4: inositol-3-phosphate synthase EC 5.5.1.5: carboxy-cis,cis-muconate cyclase EC 5.5.1.6: chalcone isomerase EC 5.5.1.7: chloromuconate cycloisomerase EC 5.5.1.8: (+)-bornyl diphosphate synthase EC 5.5.1.9: cycloeucalenol cycloisomerase EC 5.5.1.10: α-pinene-oxide decyclase EC 5.5.1.11: dichloromuconate cycloisomerase EC 5.5.1.12: copalyl diphosphate synthase EC 5.5.1.13: ent-copalyl diphosphate synthase EC 5.5.1.14: syn-copalyl-diphosphate synthase EC 5.5.1.15: terpentedienyl-diphosphate synthase EC 5.5.1.16: halimadienyl-diphosphate synthase EC 5.5.1.17: (S)-β-macrocarpene synthase EC 5.5.1.18: lycopene ε-cyclase EC 5.5.1.19: lycopene β-cyclase EC 5.5.1.20: prosolanapyrone-III cycloisomerase EC 5.5.1.21: copal-8-ol diphosphate synthase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 4.2.1.133, copal-8-ol diphosphate hydratase EC 5.5.1.22: (–)-bornyl diphosphate synthase * EC 5.5.1.23: aklanonic acid methyl ester cyclase * EC 5.5.1.24: tocopherol cyclase * EC 5.5.1.25: 3,6-anhydro-L-galactonate cycloisomerase * EC 5.5.1.26: nogalonic acid methyl ester cyclase * EC 5.5.1.27: D-galactarolactone cycloisomerase * EC 5.5.1.28: (–)-kolavenyl diphosphate synthase * EC 5.5.1.29: (+)-kolavenyl diphosphate synthase * EC 5.5.1.30: labda-7,13-dienyl diphosphate synthase * EC 5.5.1.31: hapalindole H synthase * EC
|
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"source": null,
"title": "List of EC numbers (EC 5)"
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5.5.1.32: 12-epi-hapalindole U synthase * EC 5.5.1.33: 12-epi-fischerindole U synthase * EC 5.5.1.34: (+)-cis,trans-nepetalactol synthase * EC 5.5.1.35: (+)-cis,cis-nepetalactol synthase * *No Wikipedia article == EC 5.6: Isomerases altering macromolecular conformation == === EC 5.6.1: Enzymes altering polypeptide conformation or assembly === EC 5.6.1.1: microtubule-severing ATPase EC 5.6.1.2: dynein ATPase EC 5.6.1.3: plus-end-directed kinesin ATPase EC 5.6.1.4: minus-end-directed kinesin ATPase EC 5.6.1.5: proteasome ATPase EC 5.6.1.6: channel-conductance-controlling ATPase EC 5.6.1.7: chaperonin ATPase EC 5.6.1.8: myosin ATPase EC 5.6.1.9: (R)-2-hydroxyacyl-CoA dehydratase activating ATPase * *No Wikipedia article === EC 5.6.2: Enzymes altering nucleic acid conformation === EC 5.6.2.1: DNA topoisomerase EC 5.6.2.2: DNA topoisomerase (ATP-hydrolyzing) EC 5.6.2.3: DNA 5'-3' helicase EC 5.6.2.4: DNA 3'-5' helicase == EC 5.99: Other Isomerases == === EC 5.99.1: Sole sub-subclass for isomerases that do not belong in the other subclasses === EC 5.99.1.1: thiocyanate isomerase EC 5.99.1.2: Now EC 5.6.2.1, DNA topoisomerase EC 5.99.1.3: Now EC 5.6.2.2, DNA topoisomerase (ATP-hydrolysing) EC 5.99.1.4: 2-hydroxychromene-2-carboxylate isomerase == References ==
|
{
"page_id": 5506829,
"source": null,
"title": "List of EC numbers (EC 5)"
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The molecular formula CAgNO (molar mass: 149.89 g/mol, exact mass: 148.9031 u) may refer to: Silver cyanate, cyanate salt of silver Silver fulminate, highly explosive silver salt of fulminic acid
|
{
"page_id": 61605645,
"source": null,
"title": "CAgNO"
}
|
AI/ML development platforms—such as PyTorch and Hugging Face—are software ecosystems designed to support the creation, training, deployment, and management of artificial intelligence (AI) and machine learning (ML) models.. These platforms provide tools, frameworks, and infrastructure to streamline workflows for developers, data scientists, and researchers working on AI-driven solutions. == Overview == AI/ML development platforms serve as comprehensive environments for building AI systems, ranging from simple predictive models to complex large language models (LLMs). They abstract technical complexities (e.g., distributed computing, hyperparameter tuning) while offering modular components for customization. Key users include: Developers: Building applications powered by AI/ML. Data scientists: Experimenting with algorithms and data pipelines. Researchers: Advancing state-of-the-art AI capabilities. == Key features == Modern AI/ML platforms typically include: End-to-end workflow support: Data preparation: Tools for cleaning, labeling, and augmenting datasets. Model building: Libraries for designing neural networks (e.g., PyTorch, TensorFlow integrations). Training & Optimization: Distributed training, hyperparameter tuning, and AutoML. Deployment: Exporting models to production environments (APIs, edge devices, cloud services). Scalability: Support for multi-GPU/TPU training and cloud-native infrastructure (e.g., Kubernetes). Pre-built models & templates: Repositories of pre-trained models (e.g., Hugging Face’s Model Hub) for tasks like natural language processing (NLP), computer vision, or speech recognition. Collaboration tools: Version control, experiment tracking (e.g., MLflow), and team project management. Ethical AI tools: Bias detection, explainability frameworks (e.g., SHAP, LIME), and compliance with regulations like GDPR. == Examples of platforms == == Applications == AI/ML development platforms underpin innovations in: Health care: Drug discovery, medical imaging analysis. Finance: Fraud detection, algorithmic trading. Natural language processing (NLP): Chatbots, translation systems. Autonomous systems: Self-driving cars, robotics. == Challenges == Computational costs: Training LLMs requires massive GPU/TPU resources. Data privacy: Balancing model performance with GDPR/CCPA compliance. Skill gaps: High barrier to entry for non-experts. Bias and fairness: Mitigating skewed outcomes in sensitive applications. ==
|
{
"page_id": 78972687,
"source": null,
"title": "AI/ML Development Platform"
}
|
Future trends == Democratization: Low-code/no-code platforms (e.g., Google AutoML, DataRobot). Ethical AI integration: Tools for bias mitigation and transparency. Federated learning: Training models on decentralized data. Quantum machine learning: Hybrid platforms leveraging quantum computing. == See also == Automated machine learning Large language model == References == == External links == MLflow Official Website – Open-source platform for the machine learning lifecycle. Hugging Face – Community and tools for NLP models. TensorFlow – Google's machine learning framework. Google AI Research – Publications on AI/ML advancements.
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"page_id": 78972687,
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"title": "AI/ML Development Platform"
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In the physical sciences and electrical engineering, dispersion relations describe the effect of dispersion on the properties of waves in a medium. A dispersion relation relates the wavelength or wavenumber of a wave to its frequency. Given the dispersion relation, one can calculate the frequency-dependent phase velocity and group velocity of each sinusoidal component of a wave in the medium, as a function of frequency. In addition to the geometry-dependent and material-dependent dispersion relations, the overarching Kramers–Kronig relations describe the frequency-dependence of wave propagation and attenuation. Dispersion may be caused either by geometric boundary conditions (waveguides, shallow water) or by interaction of the waves with the transmitting medium. Elementary particles, considered as matter waves, have a nontrivial dispersion relation, even in the absence of geometric constraints and other media. In the presence of dispersion, a wave does not propagate with an unchanging waveform, giving rise to the distinct frequency-dependent phase velocity and group velocity. == Dispersion == Dispersion occurs when sinusoidal waves of different wavelengths have different propagation velocities, so that a wave packet of mixed wavelengths tends to spread out in space. The speed of a plane wave, v {\displaystyle v} , is a function of the wave's wavelength λ {\displaystyle \lambda } : v = v ( λ ) . {\displaystyle v=v(\lambda ).} The wave's speed, wavelength, and frequency, f, are related by the identity v ( λ ) = λ f ( λ ) . {\displaystyle v(\lambda )=\lambda \ f(\lambda ).} The function f ( λ ) {\displaystyle f(\lambda )} expresses the dispersion relation of the given medium. Dispersion relations are more commonly expressed in terms of the angular frequency ω = 2 π f {\displaystyle \omega =2\pi f} and wavenumber k = 2 π / λ {\displaystyle k=2\pi /\lambda } . Rewriting the relation above in
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"page_id": 853778,
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these variables gives ω ( k ) = v ( k ) ⋅ k . {\displaystyle \omega (k)=v(k)\cdot k.} where we now view f as a function of k. The use of ω(k) to describe the dispersion relation has become standard because both the phase velocity ω/k and the group velocity dω/dk have convenient representations via this function. The plane waves being considered can be described by A ( x , t ) = A 0 e 2 π i x − v t λ = A 0 e i ( k x − ω t ) , {\displaystyle A(x,t)=A_{0}e^{2\pi i{\frac {x-vt}{\lambda }}}=A_{0}e^{i(kx-\omega t)},} where A is the amplitude of the wave, A0 = A(0, 0), x is a position along the wave's direction of travel, and t is the time at which the wave is described. == Plane waves in vacuum == Plane waves in vacuum are the simplest case of wave propagation: no geometric constraint, no interaction with a transmitting medium. === Electromagnetic waves in vacuum === For electromagnetic waves in vacuum, the angular frequency is proportional to the wavenumber: ω = c k . {\displaystyle \omega =ck.} This is a linear dispersion relation, in which case the waves are said to be non-dispersive. That is, the phase velocity and the group velocity are the same: v = ω k = d ω d k = c , {\displaystyle v={\frac {\omega }{k}}={\frac {d\omega }{dk}}=c,} and thus both are equal to the speed of light in vacuum, which is frequency-independent. === De Broglie dispersion relations === For de Broglie matter waves the frequency dispersion relation is non-linear: ω ( k ) ≈ m 0 c 2 ℏ + ℏ k 2 2 m 0 . {\displaystyle \omega (k)\approx {\frac {m_{0}c^{2}}{\hbar }}+{\frac {\hbar k^{2}}{2m_{0}}}\,.} The equation says the matter wave
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"page_id": 853778,
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frequency ω {\displaystyle \omega } in vacuum varies with wavenumber ( k = 2 π / λ {\displaystyle k=2\pi /\lambda } ) in the non-relativistic approximation. The variation has two parts: a constant part due to the de Broglie frequency of the rest mass ( ℏ ω 0 = m 0 c 2 {\displaystyle \hbar \omega _{0}=m_{0}c^{2}} ) and a quadratic part due to kinetic energy. ==== Derivation ==== While applications of matter waves occur at non-relativistic velocity, de Broglie applied special relativity to derive his waves. Starting from the relativistic energy–momentum relation: E 2 = ( p c ) 2 + ( m 0 c 2 ) 2 {\displaystyle E^{2}=(p{\textrm {c}})^{2}+\left(m_{0}{\textrm {c}}^{2}\right)^{2}\,} use the de Broglie relations for energy and momentum for matter waves, E = ℏ ω , p = ℏ k , {\displaystyle E=\hbar \omega \,,\quad \mathbf {p} =\hbar \mathbf {k} \,,} where ω is the angular frequency and k is the wavevector with magnitude |k| = k, equal to the wave number. Divide by ℏ {\displaystyle \hbar } and take the square root. This gives the relativistic frequency dispersion relation: ω ( k ) = k 2 c 2 + ( m 0 c 2 ℏ ) 2 . {\displaystyle \omega (k)={\sqrt {k^{2}c^{2}+\left({\frac {m_{0}c^{2}}{\hbar }}\right)^{2}}}\,.} Practical work with matter waves occurs at non-relativistic velocity. To approximate, we pull out the rest-mass dependent frequency: ω = m 0 c 2 ℏ 1 + ( k ℏ m 0 c ) 2 . {\displaystyle \omega ={\frac {m_{0}c^{2}}{\hbar }}{\sqrt {1+\left({\frac {k\hbar }{m_{0}c}}\right)^{2}}}\,.} Then we see that the ℏ / c {\displaystyle \hbar /c} factor is very small so for k {\displaystyle k} not too large, we expand 1 + x 2 ≈ 1 + x 2 / 2 , {\displaystyle {\sqrt {1+x^{2}}}\approx 1+x^{2}/2,} and multiply: ω ( k )
|
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≈ m 0 c 2 ℏ + ℏ k 2 2 m 0 . {\displaystyle \omega (k)\approx {\frac {m_{0}c^{2}}{\hbar }}+{\frac {\hbar k^{2}}{2m_{0}}}\,.} This gives the non-relativistic approximation discussed above. If we start with the non-relativistic Schrödinger equation we will end up without the first, rest mass, term. == Frequency versus wavenumber == As mentioned above, when the focus in a medium is on refraction rather than absorption—that is, on the real part of the refractive index—it is common to refer to the functional dependence of angular frequency on wavenumber as the dispersion relation. For particles, this translates to a knowledge of energy as a function of momentum. === Waves and optics === The name "dispersion relation" originally comes from optics. It is possible to make the effective speed of light dependent on wavelength by making light pass through a material which has a non-constant index of refraction, or by using light in a non-uniform medium such as a waveguide. In this case, the waveform will spread over time, such that a narrow pulse will become an extended pulse, i.e., be dispersed. In these materials, ∂ ω ∂ k {\displaystyle {\frac {\partial \omega }{\partial k}}} is known as the group velocity and corresponds to the speed at which the peak of the pulse propagates, a value different from the phase velocity. === Deep water waves === The dispersion relation for deep water waves is often written as ω = g k , {\displaystyle \omega ={\sqrt {gk}},} where g is the acceleration due to gravity. Deep water, in this respect, is commonly denoted as the case where the water depth is larger than half the wavelength. In this case the phase velocity is v p = ω k = g k , {\displaystyle v_{p}={\frac {\omega }{k}}={\sqrt {\frac {g}{k}}},} and the group velocity
|
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is v g = d ω d k = 1 2 v p . {\displaystyle v_{g}={\frac {d\omega }{dk}}={\frac {1}{2}}v_{p}.} === Waves on a string === For an ideal string, the dispersion relation can be written as ω = k T μ , {\displaystyle \omega =k{\sqrt {\frac {T}{\mu }}},} where T is the tension force in the string, and μ is the string's mass per unit length. As for the case of electromagnetic waves in vacuum, ideal strings are thus a non-dispersive medium, i.e. the phase and group velocities are equal and independent (to first order) of vibration frequency. For a nonideal string, where stiffness is taken into account, the dispersion relation is written as ω 2 = T μ k 2 + α k 4 , {\displaystyle \omega ^{2}={\frac {T}{\mu }}k^{2}+\alpha k^{4},} where α {\displaystyle \alpha } is a constant that depends on the string. === Electron band structure === In the study of solids, the study of the dispersion relation of electrons is of paramount importance. The periodicity of crystals means that many levels of energy are possible for a given momentum and that some energies might not be available at any momentum. The collection of all possible energies and momenta is known as the band structure of a material. Properties of the band structure define whether the material is an insulator, semiconductor or conductor. === Phonons === Phonons are to sound waves in a solid what photons are to light: they are the quanta that carry it. The dispersion relation of phonons is also non-trivial and important, being directly related to the acoustic and thermal properties of a material. For most systems, the phonons can be categorized into two main types: those whose bands become zero at the center of the Brillouin zone are called acoustic phonons, since
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they correspond to classical sound in the limit of long wavelengths. The others are optical phonons, since they can be excited by electromagnetic radiation. === Electron optics === With high-energy (e.g., 200 keV, 32 fJ) electrons in a transmission electron microscope, the energy dependence of higher-order Laue zone (HOLZ) lines in convergent beam electron diffraction (CBED) patterns allows one, in effect, to directly image cross-sections of a crystal's three-dimensional dispersion surface. This dynamical effect has found application in the precise measurement of lattice parameters, beam energy, and more recently for the electronics industry: lattice strain. == History == Isaac Newton studied refraction in prisms but failed to recognize the material dependence of the dispersion relation, dismissing the work of another researcher whose measurement of a prism's dispersion did not match Newton's own. Dispersion of waves on water was studied by Pierre-Simon Laplace in 1776. The universality of the Kramers–Kronig relations (1926–27) became apparent with subsequent papers on the dispersion relation's connection to causality in the scattering theory of all types of waves and particles. == See also == Ellipsometry Ultrashort pulse Waves in plasmas == Notes == == References == Ablowitz, Mark J. (2011-09-08). Nonlinear Dispersive Waves. Cambridge, UK; New York: Cambridge University Press. ISBN 978-1-107-01254-7. OCLC 714729246. == External links == Poster on CBED simulations to help visualize dispersion surfaces, by Andrey Chuvilin and Ute Kaiser Angular frequency calculator
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Marianne Grunberg-Manago (January 6, 1921 – January 3, 2013) was a Soviet-born French biochemist. Her work helped make possible key discoveries about the nature of the genetic code. Grunberg-Manago was the first woman to lead the International Union of Biochemistry and the 400-year-old French Academy of Sciences. == Early life == Grunberg-Manago was born into a family of artists who adhered to the teachings of the Swiss educational reformer Johann Pestalozzi. When she was 9 months old, her parents emigrated from the Soviet Union to France. == Education and Research == Grunberg-Manago studied biochemistry and, in 1955, while working in the lab of Spanish-American biochemist Severo Ochoa, she discovered the first nucleic-acid-synthesizing enzyme. Initially, everyone thought the new enzyme was an RNA polymerase used by E. coli cells to make long chains of RNA from separate nucleotides. Although the new enzyme could link a few nucleotides together, the reaction was highly reversible and it later became clear that the enzyme, polynucleotide phosphorylase, usually catalyzes the breakdown of RNA, not its synthesis. Nonetheless, the enzyme was extraordinarily useful and important. Almost immediately, Marshall Nirenberg and J. Heinrich Matthaei put it to use to form the first three-nucleotide RNA codons, which coded for the amino acid phenylalanine. This first step in cracking the genetic code entirely depended on the availability of Grunberg-Manago’s enzyme. In 1959, Ochoa and Arthur Kornberg won the 1959 Nobel Prize in Physiology or Medicine "for the synthesis of the nucleic acids RNA and DNA." She was elected a Foreign Honorary Member of the American Academy of Arts and Sciences in 1978, a Foreign Associate Member of the National Academy of Sciences in 1982, and an International member of the American Philosophical Society in 1992. Grunberg-Manago was the first woman president of the International Union of Biochemistry (1985–1988), and
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"page_id": 8783636,
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"title": "Marianne Grunberg-Manago"
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she was also the first woman to preside over the French Academy of Sciences (1995–1996). == Later life and death == Late in her career, Grunberg-Manago was named emeritus director of research at CNRS, France's National Center for Scientific Research. Grunberg-Manago died in January 2013, three days before her 92nd birthday. == Awards and nominations == Member of the EMBO (1964) Charles-Léopold-Mayer Prize from the French Academy of Sciences (1966) Foreign member of the American Society of Biological Chemists (1972) Member of the Federation of American Societies for Experimental Biology) Member of the French Society for biochemistry and molecular biology Foreign member of the Franklin Society (1995) Member of the Spanish Society for molecular biology Member of the Greek Society for molecular biology Member of the Executive Board of the ICSU Foreign member of the New York Academy of Sciences (1977) Foreign member of the American Academy of Arts and Sciences (1978) Foreign member of the National Academy of Sciences in the United States (1982) Honorary foreign member of the USSR Academy of Sciences (1988) Member of Academia Europaea (1988) Honorary foreign member of the Russian Academy of sciences (1991) Foreign member of the Ukrainian Academy of Sciences (1991) Grand Officer of the National Order of the Legion of Honor(2008) == References ==
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"page_id": 8783636,
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This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. == EC 4.1: Carbon-Carbon Lyases == === EC 4.1.1: Carboxy-lyases === EC 4.1.1.1: pyruvate decarboxylase EC 4.1.1.2: oxalate decarboxylase EC 4.1.1.3: Now recognized to be two enzymes EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 4.1.1.112 (oxaloacetate decarboxylase). EC 4.1.1.4: acetoacetate decarboxylase EC 4.1.1.5: acetolactate decarboxylase EC 4.1.1.6: cis-aconitate decarboxylase EC 4.1.1.7: benzoylformate decarboxylase EC 4.1.1.8: oxalyl-CoA decarboxylase EC 4.1.1.9: malonyl-CoA decarboxylase EC 4.1.1.10: Now included with EC 4.1.1.12, aspartate 4-decarboxylase EC 4.1.1.11: aspartate 1-decarboxylase EC 4.1.1.12: aspartate 4-decarboxylase EC 4.1.1.13: deleted EC 4.1.1.14: valine decarboxylase EC 4.1.1.15: glutamate decarboxylase EC 4.1.1.16: hydroxyglutamate decarboxylase EC 4.1.1.17: ornithine decarboxylase EC 4.1.1.18: lysine decarboxylase EC 4.1.1.19: arginine decarboxylase EC 4.1.1.20: diaminopimelate decarboxylase EC 4.1.1.21: phosphoribosylaminoimidazole carboxylase EC 4.1.1.22: histidine decarboxylase EC 4.1.1.23: orotidine-5′-phosphate decarboxylase EC 4.1.1.24: aminobenzoate decarboxylase EC 4.1.1.25: tyrosine decarboxylase EC 4.1.1.26: Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase EC 4.1.1.27: Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase EC 4.1.1.28: aromatic-L-amino-acid decarboxylase EC 4.1.1.29: sulfoalanine decarboxylase EC 4.1.1.30: pantothenoylcysteine decarboxylase EC 4.1.1.31: phosphoenolpyruvate carboxylase EC 4.1.1.32: phosphoenolpyruvate carboxykinase (GTP) EC 4.1.1.33: diphosphomevalonate decarboxylase EC 4.1.1.34: dehydro-L-gulonate decarboxylase EC 4.1.1.35: UDP-glucuronate decarboxylase EC 4.1.1.36: phosphopantothenoylcysteine decarboxylase EC 4.1.1.37: uroporphyrinogen decarboxylase EC 4.1.1.38: phosphoenolpyruvate carboxykinase (diphosphate) EC 4.1.1.39: ribulose-bisphosphate carboxylase EC 4.1.1.40: hydroxypyruvate decarboxylase EC 4.1.1.41: Now EC 7.2.4.3, (S)-methylmalonyl-CoA decarboxylase EC 4.1.1.42: carnitine decarboxylase EC 4.1.1.43: phenylpyruvate decarboxylase EC 4.1.1.44: 4-carboxymuconolactone decarboxylase EC 4.1.1.45: aminocarboxymuconate-semialdehyde decarboxylase EC 4.1.1.46: o-pyrocatechuate decarboxylase EC 4.1.1.47: tartronate-semialdehyde synthase EC 4.1.1.48: indole-3-glycerol-phosphate synthase EC 4.1.1.49: phosphoenolpyruvate carboxykinase (ATP) EC 4.1.1.50: adenosylmethionine decarboxylase
|
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EC 4.1.1.51: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase EC 4.1.1.52: 6-methylsalicylate decarboxylase EC 4.1.1.53: phenylalanine decarboxylase EC 4.1.1.54: dihydroxyfumarate decarboxylase EC 4.1.1.55: 4,5-dihydroxyphthalate decarboxylase EC 4.1.1.56: 3-oxolaurate decarboxylase EC 4.1.1.57: methionine decarboxylase EC 4.1.1.58: orsellinate decarboxylase EC 4.1.1.59: gallate decarboxylase EC 4.1.1.60: stipitatonate decarboxylase EC 4.1.1.61: 4-hydroxybenzoate decarboxylase EC 4.1.1.62: gentisate decarboxylase EC 4.1.1.63: protocatechuate decarboxylase EC 4.1.1.64: 2,2-dialkylglycine decarboxylase (pyruvate) EC 4.1.1.65: phosphatidylserine decarboxylase EC 4.1.1.66: uracil-5-carboxylate decarboxylase EC 4.1.1.67: UDP-galacturonate decarboxylase EC 4.1.1.68: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase EC 4.1.1.69: 3,4-dihydroxyphthalate decarboxylase EC 4.1.1.70: Now EC 7.2.4.5, glutaconyl-CoA decarboxylase EC 4.1.1.71: 2-oxoglutarate decarboxylase EC 4.1.1.72: branched-chain-2-oxoacid decarboxylase EC 4.1.1.73: tartrate decarboxylase EC 4.1.1.74: indolepyruvate decarboxylase EC 4.1.1.75: 5-guanidino-2-oxopentanoate decarboxylase EC 4.1.1.76: arylmalonate decarboxylase EC 4.1.1.77: 4-oxalocrotonate decarboxylase EC 4.1.1.78: acetylenedicarboxylate decarboxylase EC 4.1.1.79: sulfopyruvate decarboxylase EC 4.1.1.80: 4-hydroxyphenylpyruvate decarboxylase EC 4.1.1.81: threonine-phosphate decarboxylase EC 4.1.1.82: phosphonopyruvate decarboxylase EC 4.1.1.83: 4-hydroxyphenylacetate decarboxylase EC 4.1.1.84: D-dopachrome decarboxylase EC 4.1.1.85: 3-dehydro-L-gulonate-6-phosphate decarboxylase EC 4.1.1.86: diaminobutyrate decarboxylase EC 4.1.1.87: malonyl-S-ACP decarboxylase EC 4.1.1.88: biotin-independent malonate decarboxylase EC 4.1.1.89: Now EC 7.2.4.4 EC 7.2.4.4, biotin-dependent malonate decarboxylase EC 4.1.1.90: peptidyl-glutamate 4-carboxylase EC 4.1.1.91: salicylate decarboxylase EC 4.1.1.92: indole-3-carboxylate decarboxylase EC 4.1.1.93: pyrrole-2-carboxylate decarboxylase EC 4.1.1.94: ethylmalonyl-CoA decarboxylase EC 4.1.1.95: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase EC 4.1.1.96: carboxynorspermidine decarboxylase EC 4.1.1.97: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase * EC 4.1.1.98: 4-hydroxy-3-polyprenylbenzoate decarboxylase * EC 4.1.1.99: phosphomevalonate decarboxylase * EC 4.1.1.100: prephenate decarboxylase * EC 4.1.1.101: malolactic enzyme * EC 4.1.1.102: phenacrylate decarboxylase * EC 4.1.1.103: γ-resorcylate decarboxylase * EC 4.1.1.104: 3-dehydro-4-phosphotetronate decarboxylase * EC 4.1.1.105: L-tryptophan decarboxylase * EC 4.1.1.106: fatty acid photodecarboxylase EC 4.1.1.107: 3,4-dihydroxyphenylacetaldehyde synthase * EC 4.1.1.108: 4-hydroxyphenylacetaldehyde synthase * EC 4.1.1.109: phenylacetaldehyde synthase * EC 4.1.1.110: bisphosphomevalonate decarboxylase * EC 4.1.1.111: siroheme decarboxylase * EC 4.1.1.112: oxaloacetate decarboxylase * EC 4.1.1.113: trans-aconitate decarboxylase * EC 4.1.1.114: cis-3-alkyl-4-alkyloxetan-2-one decarboxylase * EC 4.1.1.115: indoleacetate decarboxylase * EC 4.1.1.116: D-ornithine/D-lysine decarboxylase * EC 4.1.1.117: 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate
|
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"page_id": 5506837,
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decarboxylase * EC 4.1.1.118: isophthalyl-CoA decarboxylase * EC 4.1.1.119: phenylacetate decarboxylase * EC 4.1.1.120: 3-oxoisoapionate decarboxylase * EC 4.1.1.121: 3-oxoisoapionate-4-phosphate decarboxylase * *No Wikipedia article === EC 4.1.2: Aldehyde-lyases === EC 4.1.2.1: Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase EC 4.1.2.2: ketotetrose-phosphate aldolase EC 4.1.2.3: deleted, was pentosealdolase. EC 4.1.2.4: deoxyribose-phosphate aldolase EC 4.1.2.5: L-threonine aldolase EC 4.1.2.6: Deleted, reaction is due to EC 2.1.2.1, glycine hydroxymethyltransferase EC 4.1.2.7: Now included with EC 4.1.2.13 fructose-bisphosphate aldolase EC 4.1.2.8: indole-3-glycerol-phosphate lyase EC 4.1.2.9: phosphoketolase EC 4.1.2.10: (R)-mandelonitrile lyase EC 4.1.2.11: hydroxymandelonitrile lyase EC 4.1.2.12: 2-dehydropantoate aldolase EC 4.1.2.13: fructose-bisphosphate aldolase EC 4.1.2.14: 2-dehydro-3-deoxy-phosphogluconate aldolase EC 4.1.2.15: Now EC 2.5.1.54, 3-deoxy-7-phosphoheptulonate synthase EC 4.1.2.16: Now EC 2.5.1.55, 3-deoxy-8-phosphooctulonate synthase EC 4.1.2.17: L-fuculose-phosphate aldolase EC 4.1.2.18: 2-dehydro-3-deoxy-L-pentonate aldolase EC 4.1.2.19: rhamnulose-1-phosphate aldolase EC 4.1.2.20: 2-dehydro-3-deoxyglucarate aldolase EC 4.1.2.21: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase EC 4.1.2.22: fructose-6-phosphate phosphoketolase EC 4.1.2.23: 3-deoxy-D-manno-octulosonate aldolase EC 4.1.2.24: dimethylaniline-N-oxide aldolase EC 4.1.2.25: dihydroneopterin aldolase EC 4.1.2.26: phenylserine aldolase EC 4.1.2.27: sphinganine-1-phosphate aldolase EC 4.1.2.28: 2-dehydro-3-deoxy-D-pentonate aldolase EC 4.1.2.29: 5-dehydro-2-deoxyphosphogluconate aldolase EC 4.1.2.30: Now EC 1.14.14.32}, 17α-hydroxyprogesterone deacetylase EC 4.1.2.31: Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase EC 4.1.2.32: trimethylamine-oxide aldolase EC 4.1.2.33: fucosterol-epoxide lyase EC 4.1.2.34: 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase EC 4.1.2.35: propioin synthase EC 4.1.2.36: lactate aldolase EC 4.1.2.37: Now covered by EC 4.1.2.46 [aliphatic (R)-hydroxynitrile lyase] and EC 4.1.2.47 [(S)-hydroxynitrile ketone-lyase (cyanide forming)] EC 4.1.2.38: benzoin aldolase EC 4.1.2.39: Deleted, identical to EC 4.1.2.37, hydroxynitrilase EC 4.1.2.40: tagatose-bisphosphate aldolase EC 4.1.2.41: Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase EC 4.1.2.42: D-threonine aldolase EC 4.1.2.43: 3-hexulose-6-phosphate synthase EC 4.1.2.44: benzoyl-CoA-dihydrodiol lyase EC 4.1.2.45: trans-o-hydroxybenzylidenepyruvate hydratase-aldolase EC 4.1.2.46: aliphatic (R)-hydroxynitrile lyase EC 4.1.2.47: (S)-hydroxynitrile lyase EC 4.1.2.48: low-specificity L-threonine aldolase EC 4.1.2.49: L-allo-threonine aldolase EC 4.1.2.50: 6-carboxytetrahydropterin synthase * EC 4.1.2.50: 6-carboxytetrahydropterin synthase * * EC 4.1.2.51: 2-dehydro-3-deoxy-D-gluconate aldolase * * EC 4.1.2.52:
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"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
4-hydroxy-2-oxoheptanedioate aldolase * * EC 4.1.2.53: 2-keto-3-deoxy-L-rhamnonate aldolase * * EC 4.1.2.54: L-threo-3-deoxy-hexylosonate aldolase * * EC 4.1.2.55: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase * * EC 4.1.2.56: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate synthase * * EC 4.1.2.57: sulfofructosephosphate aldolase * * EC 4.1.2.58: 2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase * * EC 4.1.2.59: dihydroneopterin phosphate aldolase * * EC 4.1.2.60: dihydroneopterin triphosphate aldolase * * EC 4.1.2.61: feruloyl-CoA hydratase/lyase * * EC 4.1.2.62: 5-deoxyribulose 1-phosphate aldolase * * EC 4.1.2.63: 2-hydroxyacyl-CoA lyase * *No Wikipedia article === EC 4.1.3: Oxo-Acid-Lyases === EC 4.1.3.1: isocitrate lyase EC 4.1.3.2: Now EC 2.3.3.9, malate synthase EC 4.1.3.3: N-acetylneuraminate lyase EC 4.1.3.4: hydroxymethylglutaryl-CoA lyase EC 4.1.3.5: Now EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase EC 4.1.3.6: citrate (pro-3S)-lyase EC 4.1.3.7: Now EC 2.3.3.1, citrate (Si)-synthase EC 4.1.3.8: Now EC 2.3.3.8, ATP citrate synthase EC 4.1.3.9: Now EC 2.3.3.11, 2-hydroxyglutarate synthase EC 4.1.3.10: Now EC 2.3.3.7, 3-ethylmalate synthase EC 4.1.3.11: Now EC 2.3.3.12, 3-propylmalate synthase EC 4.1.3.12: Now EC 2.3.3.13, 2-isopropylmalate synthase EC 4.1.3.13: oxalomalate lyase EC 4.1.3.14: L-erythro-3-hydroxyaspartate aldolase EC 4.1.3.15: Now EC 2.2.1.5, 2-hydroxy-3-oxoadipate synthase EC 4.1.3.16: 4-hydroxy-2-oxoglutarate aldolase EC 4.1.3.17: 4-hydroxy-4-methyl-2-oxoglutarate aldolase EC 4.1.3.18: Now EC 2.2.1.6, acetolactate synthase EC 4.1.3.19: Now EC 2.5.1.56 EC 4.1.3.20: Now EC 2.5.1.57 EC 4.1.3.21: Now EC 2.3.3.14 EC 4.1.3.22: citramalate lyase EC 4.1.3.23: Now EC 2.3.3.2, decylcitrate synthase EC 4.1.3.24: malyl-CoA lyase EC 4.1.3.25: (S)-citramalyl-CoA lyase EC 4.1.3.26: 3-hydroxy-3-isohexenylglutaryl-CoA lyase EC 4.1.3.27: anthranilate synthase EC 4.1.3.28: Now EC 2.3.3.3, citrate (Re)-synthase EC 4.1.3.29: Now EC 2.3.3.4, decylhomocitrate synthase EC 4.1.3.30: methylisocitrate lyase EC 4.1.3.31: Now EC 2.3.3.5, 2-methylcitrate synthase EC 4.1.3.32: 2,3-dimethylmalate lyase EC 4.1.3.33: Now EC 2.3.3.6 EC 4.1.3.34: citryl-CoA lyase EC 4.1.3.35: (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase EC 4.1.3.36: naphthoate synthase EC 4.1.3.37: Now EC 2.2.1.7, 1-deoxy-D-xylulose 5-phosphate synthase EC 4.1.3.38: aminodeoxychorismate lyase EC 4.1.3.39: 4-hydroxy-2-oxovalerate aldolase EC 4.1.3.40: chorismate lyase EC 4.1.3.41: 3-hydroxy-D-aspartate aldolase EC 4.1.3.42: (4S)-4-hydroxy-2-oxoglutarate aldolase *
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
EC 4.1.3.43: 4-hydroxy-2-oxohexanoate aldolase * EC 4.1.3.44: tRNA 4-demethylwyosine synthase (AdoMet-dependent) * EC 4.1.3.45: 3-hydroxybenzoate synthase * EC 4.1.3.46: (R)-citramalyl-CoA lyase * *No Wikipedia article === EC 4.1.99: Other Carbon-Carbon Lyases === EC 4.1.99.1: tryptophanase EC 4.1.99.2: tyrosine phenol-lyase EC 4.1.99.3: deoxyribodipyrimidine photo-lyase EC 4.1.99.4: Now EC 3.5.99.7, 1-aminocyclopropane-1-carboxylate deaminase EC 4.1.99.5: octadecanal decarbonylase EC 4.1.99.6: Now EC 4.2.3.6, trichodiene synthase EC 4.1.99.7: Now EC 4.2.3.9, aristolochene synthase EC 4.1.99.8: Now EC 4.2.3.14, pinene synthase EC 4.1.99.9: Now EC 4.2.3.15, myrcene synthase EC 4.1.99.10: Now EC 4.2.3.16, (4S)-limonene synthase EC 4.1.99.11: benzylsuccinate synthase EC 4.1.99.12: 3,4-dihydroxy-2-butanone-4-phosphate synthase EC 4.1.99.13: (6-4)DNA photolyase EC 4.1.99.14: spore photoproduct lyase EC 4.1.99.15: The activity is covered by EC 4.1.99.14, spore photoproduct lyase EC 4.1.99.16: geosmin synthase EC 4.1.99.17: phosphomethylpyrimidine synthase EC 4.1.99.18: Now known to be catalysed by the combined effect of EC 4.1.99.22, GTP 3,8-cyclase, and EC 4.6.1.17, cyclic pyranopterin monophosphate synthase EC 4.1.99.19: 2-iminoacetate synthase EC 4.1.99.20: 3-amino-4-hydroxybenzoate synthase * EC 4.1.99.21: Now EC 4.2.3.153 (5-formylfuran-3-yl)methyl phosphate synthase. EC 4.1.99.22: GTP 3′,8-cyclase * EC 4.1.99.23: 5-hydroxybenzimidazole synthase * EC 4.1.99.24: L-tyrosine isonitrile synthase * EC 4.1.99.25: L-tryptophan isonitrile synthase * EC 4.1.99.26: 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one * *No Wikipedia article == EC 4.2: Carbon-Oxygen Lyases == === EC 4.2.1: Hydro-lyases === EC 4.2.1.1: carbonic anhydrase EC 4.2.1.2: fumarate hydratase EC 4.2.1.3: aconitate hydratase EC 4.2.1.4: Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase EC 4.2.1.5: arabinonate dehydratase EC 4.2.1.6: galactonate dehydratase EC 4.2.1.7: altronate dehydratase EC 4.2.1.8: mannonate dehydratase EC 4.2.1.9: dihydroxy-acid dehydratase EC 4.2.1.10: 3-dehydroquinate dehydratase EC 4.2.1.11: phosphopyruvate hydratase (enolase) EC 4.2.1.12: phosphogluconate dehydratase EC 4.2.1.13: Now EC 4.3.1.17, L-serine ammonia-lyase EC 4.2.1.14: Now EC 4.3.1.18, D-serine ammonia-lyase EC 4.2.1.15: Identical with EC 4.4.1.1 cystathionine γ-lyase EC 4.2.1.16: Now EC 4.3.1.19, threonine ammonia-lyase EC 4.2.1.17: enoyl-CoA hydratase EC
|
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"source": null,
"title": "List of EC numbers (EC 4)"
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4.2.1.18: methylglutaconyl-CoA hydratase EC 4.2.1.19: imidazoleglycerol-phosphate dehydratase EC 4.2.1.20: tryptophan synthase EC 4.2.1.21: Now EC 4.2.1.22 cystathionine β-synthase EC 4.2.1.22: cystathionine β-synthase EC 4.2.1.23: deleted, the reaction was due to a side-reaction of EC 4.2.1.22 cystathionine β-synthase EC 4.2.1.24: porphobilinogen synthase EC 4.2.1.25: L-arabinonate dehydratase EC 4.2.1.26: identical to EC 4.3.1.9, glucosaminate ammonia-lyase EC 4.2.1.27: acetylenecarboxylate hydratase EC 4.2.1.28: propanediol dehydratase EC 4.2.1.29: Now EC 4.99.1.6, indoleacetaldoxime dehydratase EC 4.2.1.30: glycerol dehydratase EC 4.2.1.31: maleate hydratase EC 4.2.1.32: L(+)-tartrate dehydratase EC 4.2.1.33: 3-isopropylmalate dehydratase EC 4.2.1.34: (S)-2-methylmalate dehydratase EC 4.2.1.35: (R)-2-methylmalate dehydratase EC 4.2.1.36: homoaconitate hydratase EC 4.2.1.37: Now EC 3.3.2.4, trans-epoxysuccinate hydrolase EC 4.2.1.38: Now EC 4.3.1.20, erythro-3-hydroxyaspartate ammonia-lyase EC 4.2.1.39: gluconate dehydratase EC 4.2.1.40: glucarate dehydratase EC 4.2.1.41: 5-dehydro-4-deoxyglucarate dehydratase EC 4.2.1.42: galactarate dehydratase EC 4.2.1.43: 2-dehydro-3-deoxy-L-arabinonate dehydratase EC 4.2.1.44: myo-inosose-2 dehydratase EC 4.2.1.45: CDP-glucose 4,6-dehydratase EC 4.2.1.46: dTDP-glucose 4,6-dehydratase EC 4.2.1.47: GDP-mannose 4,6-dehydratase EC 4.2.1.48: D-glutamate cyclase EC 4.2.1.49: urocanate hydratase EC 4.2.1.50: pyrazolylalanine synthase EC 4.2.1.51: prephenate dehydratase EC 4.2.1.52: Now EC 4.3.3.7, 4-hydroxy-2,3,4,5-tetrahydrodipicolinate synthase. EC 4.2.1.53: oleate hydratase EC 4.2.1.54: lactoyl-CoA dehydratase EC 4.2.1.55: 3-hydroxybutyryl-CoA dehydratase EC 4.2.1.56: itaconyl-CoA hydratase EC 4.2.1.57: isohexenylglutaconyl-CoA hydratase EC 4.2.1.58: The reaction described is covered by EC 4.2.1.59 EC 4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase EC 4.2.1.60: 3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase EC 4.2.1.61: The reaction described is covered by EC 4.2.1.59. EC 4.2.1.62: 5α-hydroxysteroid dehydratase EC 4.2.1.63: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) EC 4.2.1.64: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) EC 4.2.1.65: 3-cyanoalanine hydratase EC 4.2.1.66: cyanide hydratase EC 4.2.1.67: D-fuconate dehydratase EC 4.2.1.68: L-fuconate dehydratase EC 4.2.1.69: cyanamide hydratase EC 4.2.1.70: pseudouridylate synthase EC 4.2.1.71: identical to EC 4.2.1.27, acetylenecarboxylate hydratase EC 4.2.1.72: Now EC 4.1.1.78, acetylenedicarboxylate decarboxylase EC 4.2.1.73:
|
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"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
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protoaphin-aglucone dehydratase (cyclizing) EC 4.2.1.74: long-chain-enoyl-CoA hydratase EC 4.2.1.75: uroporphyrinogen-III synthase EC 4.2.1.76: UDP-glucose 4,6-dehydratase EC 4.2.1.77: trans-L-3-hydroxyproline dehydratase EC 4.2.1.78: (S)-norcoclaurine synthase EC 4.2.1.79: 2-methylcitrate dehydratase EC 4.2.1.80: 2-oxopent-4-enoate hydratase EC 4.2.1.81: D(-)-tartrate dehydratase EC 4.2.1.82: xylonate dehydratase EC 4.2.1.83: 4-oxalmesaconate hydratase EC 4.2.1.84: nitrile hydratase EC 4.2.1.85: dimethylmaleate hydratase EC 4.2.1.86: identical to EC 4.2.1.98, 16α-hydroxyprogesterone dehydratase EC 4.2.1.87: octopamine dehydratase EC 4.2.1.88: synephrine dehydratase EC 4.2.1.89: The activity has now been shown to be due to EC 2.8.3.21, L-carnitine CoA-transferase and EC 4.2.1.149, crotonobetainyl-CoA hydratase EC 4.2.1.90: L-rhamnonate dehydratase EC 4.2.1.91: arogenate dehydratase EC 4.2.1.92: hydroperoxide dehydratase EC 4.2.1.93: ATP-dependent NAD(P)H-hydrate dehydratase EC 4.2.1.94: scytalone dehydratase EC 4.2.1.95: kievitone hydratase EC 4.2.1.96: 4a-hydroxytetrahydrobiopterin dehydratase EC 4.2.1.97: phaseollidin hydratase EC 4.2.1.98: 16α-hydroxyprogesterone dehydratase EC 4.2.1.99: 2-methylisocitrate dehydratase EC 4.2.1.100: cyclohexa-1,5-dienecarbonyl-CoA hydratase EC 4.2.1.101: Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase EC 4.2.1.102: Now EC 4.2.1.100, cyclohexa-1,5-dienecarbonyl-CoA hydratase EC 4.2.1.103: cyclohexyl-isocyanide hydratase EC 4.2.1.104: cyanase EC 4.2.1.105: 2-hydroxyisoflavanone dehydratase EC 4.2.1.106: bile-acid 7α-dehydratase EC 4.2.1.107: 3α,7α,12α-trihydroxy-5β-cholest-24-enoyl-CoA hydratase EC 4.2.1.108: ectoine synthase EC 4.2.1.109: methylthioribulose 1-phosphate dehydratase EC 4.2.1.110: aldos-2-ulose dehydratase EC 4.2.1.111: 1,5-anhydro-D-fructose dehydratase EC 4.2.1.112: acetylene hydratase EC 4.2.1.113: o-succinylbenzoate synthase EC 4.2.1.114: methanogen homoaconitase EC 4.2.1.115: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting) EC 4.2.1.116: 3-hydroxypropionyl-CoA dehydratase EC 4.2.1.117: 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) EC 4.2.1.118: 3-dehydroshikimate dehydratase EC 4.2.1.119: enoyl-CoA hydratase 2 EC 4.2.1.120: 4-hydroxybutanoyl-CoA dehydratase EC 4.2.1.121: colneleate synthase EC 4.2.1.122: tryptophan synthase (indole-salvaging) EC 4.2.1.123: tetrahymanol synthase EC 4.2.1.124: arabidiol synthase EC 4.2.1.125: dammarenediol II synthase EC 4.2.1.126: N-acetylmuramic acid 6-phosphate etherase EC 4.2.1.127: linalool dehydratase EC 4.2.1.128: lupan-3β,20-diol synthase EC 4.2.1.129: squalene—hopanol cyclase EC 4.2.1.130: D-lactate dehydratase EC 4.2.1.131: carotenoid 1,2-hydratase EC 4.2.1.132: 2-hydroxyhexa-2,4-dienoate hydratase EC 4.2.1.133: copal-8-ol diphosphate hydratase EC 4.2.1.134: very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase EC 4.2.1.135: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) EC 4.2.1.136: ADP-dependent NAD(P)H-hydrate dehydratase EC 4.2.1.137: sporulenol
|
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"page_id": 5506837,
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"title": "List of EC numbers (EC 4)"
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synthase EC 4.2.1.138: (+)-Caryolan-1-ol synthase EC 4.2.1.139: pterocarpan synthase * EC 4.2.1.140: gluconate/galactonate dehydratase * EC 4.2.1.141: 2-dehydro-3-deoxyD-arabinonate dehydratase * EC 4.2.1.142: 5′-oxoaverantin cyclase * EC 4.2.1.143: versicolorin B synthase * EC 4.2.1.144: 3-amino-5-hydroxybenzoate synthase * EC 4.2.1.145: capreomycidine synthase * EC 4.2.1.146: L-galactonate dehydratase * EC 4.2.1.147: 5,6,7,8-tetrahydromethanopterin hydro-lyase * EC 4.2.1.148: 2-methylfumaryl-CoA hydratase * EC 4.2.1.149: crotonobetainyl-CoA hydratase * EC 4.2.1.150: short-chain-enoyl-CoA hydratase * EC 4.2.1.151: chorismate dehydratase * EC 4.2.1.152: hydroperoxy icosatetraenoate dehydratase * EC 4.2.1.153: 3-methylfumaryl-CoA hydratase * EC 4.2.1.154: tetracenomycin F2 cyclase * EC 4.2.1.155: (methylthio)acryloyl-CoA hydratase * EC 4.2.1.156: L-talarate dehydratase * EC 4.2.1.157: (R)-2-hydroxyisocaproyl-CoA dehydratase * EC 4.2.1.158: galactarate dehydratase (D-threo-forming) * EC 4.2.1.159: dTDP-4-dehydro-6-deoxy-α-glucopyranose 2,3-dehydratase * EC 4.2.1.160: 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one isomerase/dehydratase * EC 4.2.1.161: bisanhydrobacterioruberin hydratase * EC 4.2.1.162: 6-deoxy-6-sulfo-D-gluconate dehydratase * EC 4.2.1.163: 2-oxo-hept-4-ene-1,7-dioate hydratase * EC 4.2.1.164: dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase * EC 4.2.1.165: chlorophyllide a 31-hydratase * EC 4.2.1.166: phosphinomethylmalate isomerase * EC 4.2.1.167: (R)-2-hydroxyglutaryl-CoA dehydratase * EC 4.2.1.168: GDP-4-dehydro-6-deoxy-α-D-mannose 3-dehydratase * EC 4.2.1.169: 3-vinyl bacteriochlorophyllide d 31-hydratase * EC 4.2.1.170: 2-(ω-methylthio)alkylmalate dehydratase * EC 4.2.1.171: cis-L-3-hydroxyproline dehydratase * EC 4.2.1.172: trans-4-hydroxy-L-proline dehydratase * EC 4.2.1.173: ent-8α-hydroxylabd-13-en-15-yl diphosphate synthase * EC 4.2.1.174: peregrinol diphosphate synthase * EC 4.2.1.175: (R)-3-(aryl)lactoyl-CoA dehydratase * EC 4.2.1.176: L-lyxonate dehydratase * EC 4.2.1.177: (2S)-3-sulfopropanediol dehydratase * *No Wikipedia article === EC 4.2.2: Acting on Polysaccharides === EC 4.2.2.1: hyaluronate lyase EC 4.2.2.2: pectate lyase EC 4.2.2.3: mannuronate-specific alginate lyase EC 4.2.2.4: Now known to comprise two enzymes: EC 4.2.2.20, chondroitin-sulfate-ABC endolyase and EC 4.2.2.21, chondroitin-sulfate-ABC exolyase EC 4.2.2.5: chondroitin AC lyase EC 4.2.2.6: oligogalacturonide lyase EC 4.2.2.7: heparin lyase EC 4.2.2.8: heparin-sulfate lyase EC 4.2.2.9: pectate disaccharide-lyase EC 4.2.2.10: pectin lyase EC 4.2.2.11: guluronate-specific alginate lyase EC 4.2.2.12: xanthan lyase EC 4.2.2.13: exo-(1→4)-α-D-glucan lyase EC 4.2.2.14: glucuronan lyase EC 4.2.2.15: anhydrosialidase EC 4.2.2.16: levan fructotransferase (DFA-IV-forming) EC
|
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"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
4.2.2.17: inulin fructotransferase (DFA-I-forming) EC 4.2.2.18: inulin fructotransferase (DFA-III-forming) EC 4.2.2.19: chondroitin B lyase EC 4.2.2.20: chondroitin-sulfate-ABC endolyase EC 4.2.2.21: chondroitin-sulfate-ABC exolyase EC 4.2.2.22: pectate trisaccharide-lyase EC 4.2.2.23: rhamnogalacturonan endolyase EC 4.2.2.24: rhamnogalacturonan exolyase EC 4.2.2.25: gellan lyase EC 4.2.2.26: oligo-alginate lyase * EC 4.2.2.27: pectin monosaccharide-lyase * *No Wikipedia article === EC 4.2.3: Acting on phosphates === EC 4.2.3.1: threonine synthase EC 4.2.3.2: ethanolamine-phosphate phospho-lyase EC 4.2.3.3: methylglyoxal synthase EC 4.2.3.4: 3-dehydroquinate synthase EC 4.2.3.5: chorismate synthase EC 4.2.3.6: trichodiene synthase EC 4.2.3.7: pentalenene synthase EC 4.2.3.8: casbene synthase EC 4.2.3.9: aristolochene synthase EC 4.2.3.10: (–)-endo-fenchol synthase EC 4.2.3.11: sabinene-hydrate synthase EC 4.2.3.12: 6-pyruvoyltetrahydropterin synthase EC 4.2.3.13: (+)-δ-cadinene synthase EC 4.2.3.14: Now covered by EC 4.2.3.119, (–)-α-pinene synthase, and EC 4.2.3.120, (–)-β-pinene synthase EC 4.2.3.15: myrcene synthase EC 4.2.3.16: (4S)-limonene synthase EC 4.2.3.17: taxadiene synthase EC 4.2.3.18: abietadiene synthase EC 4.2.3.19: ent-kaurene synthase EC 4.2.3.20: (R)-limonene synthase EC 4.2.3.21: vetispiradiene synthase EC 4.2.3.22: germacradienol synthase EC 4.2.3.23: germacrene-A synthase EC 4.2.3.24: amorpha-4,11-diene synthase EC 4.2.3.25: S-linalool synthase EC 4.2.3.26: R-linalool synthase EC 4.2.3.27: isoprene synthase EC 4.2.3.28: ent-cassa-12,15-diene synthase EC 4.2.3.29: ent-sandaracopimaradiene synthase EC 4.2.3.30: ent-pimara-8(14),15-diene synthase EC 4.2.3.31: ent-pimara-9(11),15-diene synthase EC 4.2.3.32: levopimaradiene synthase EC 4.2.3.33: stemar-13-ene synthase EC 4.2.3.34: stemod-13(17)-ene synthase EC 4.2.3.35: syn-pimara-7,15-diene synthase EC 4.2.3.36: terpentetriene synthase EC 4.2.3.37: epi-isozizaene synthase EC 4.2.3.38: α-bisabolene synthase EC 4.2.3.39: epi-cedrol synthase EC 4.2.3.40: (Z)-γ-bisabolene synthase EC 4.2.3.41: elisabethatriene synthase EC 4.2.3.42: aphidicolan-16β-ol synthase EC 4.2.3.43: fusicocca-2,10(14)-diene synthase EC 4.2.3.44: isopimara-7,15-diene synthase EC 4.2.3.45: phyllocladan-16α-ol synthase EC 4.2.3.46: α-farnesene synthase EC 4.2.3.47: β-farnesene synthase EC 4.2.3.48: (3S,6E)-nerolidol synthase EC 4.2.3.49: (3R,6E)-nerolidol synthase EC 4.2.3.50: (+)-α-santalene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] EC 4.2.3.51: β-phellandrene synthase (neryl-diphosphate-cyclizing) EC 4.2.3.52: (4S)-β-phellandrene synthase (geranyl-diphosphate-cyclizing) EC 4.2.3.53: (+)-endo-β-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] EC 4.2.3.54: (–)-endo-α-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] EC 4.2.3.55: (S)-β-bisabolene synthase EC
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
4.2.3.56: γ-humulene synthase EC 4.2.3.57: (–)-β-caryophyllene synthase EC 4.2.3.58: longifolene synthase EC 4.2.3.59: (E)-γ-bisabolene synthase EC 4.2.3.60: germacrene C synthase EC 4.2.3.61: 5-epiaristolochene synthase EC 4.2.3.62: (–)-γ-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing] EC 4.2.3.63: (+)-cubenene synthase EC 4.2.3.64: (+)-epicubenol synthase EC 4.2.3.65: zingiberene synthase EC 4.2.3.66: β-selinene cyclase EC 4.2.3.67: cis-muuroladiene synthase EC 4.2.3.68: β-eudesmol synthase EC 4.2.3.69: (+)-α-barbatene synthase EC 4.2.3.70: patchoulol synthase EC 4.2.3.71: (E,E)-germacrene B synthase EC 4.2.3.72: α-gurjunene synthase EC 4.2.3.73: valencene synthase EC 4.2.3.74: presilphiperfolanol synthase EC 4.2.3.75: (–)-germacrene D synthase EC 4.2.3.76: (+)-δ-selinene synthase EC 4.2.3.77: (+)-germacrene D synthase EC 4.2.3.78: β-chamigrene synthase EC 4.2.3.79: thujopsene synthase EC 4.2.3.80: α-longipinene synthase EC 4.2.3.81: exo-α-bergamotene synthase EC 4.2.3.82: α-santalene synthase EC 4.2.3.83: β-santalene synthase EC 4.2.3.84: 10-epi-γ-eudesmol synthase EC 4.2.3.85: α-eudesmol synthase EC 4.2.3.86: 7-epi-α-selinene synthase EC 4.2.3.87: α-guaiene synthase EC 4.2.3.88: viridiflorene synthase EC 4.2.3.89: (+)-β-caryophyllene synthase EC 4.2.3.90: 5-epi-α-selinene synthase EC 4.2.3.91: cubebol synthase EC 4.2.3.92: (+)-γ-cadinene synthase EC 4.2.3.93: δ-guaiene synthase EC 4.2.3.94: γ-curcumene synthase EC 4.2.3.95: (–)-α-cuprenene synthase EC 4.2.3.96: avermitilol synthase EC 4.2.3.97: (–)-δ-cadinene synthase EC 4.2.3.98: (+)-T-muurolol synthase EC 4.2.3.99: labdatriene synthase EC 4.2.3.100: bicyclogermacrene synthase EC 4.2.3.101: 7-epi-sesquithujene synthase EC 4.2.3.102: sesquithujene synthase EC 4.2.3.103: ent-isokaurene synthase EC 4.2.3.104: α-humulene synthase EC 4.2.3.105: tricyclene synthase EC 4.2.3.106: (E)-β-ocimene synthase EC 4.2.3.107: (+)-car-3-ene synthase EC 4.2.3.108: 1,8-cineole synthase EC 4.2.3.109: (–)-sabinene synthase EC 4.2.3.110: (+)-sabinene synthase EC 4.2.3.111: (–)-α-terpineol synthase EC 4.2.3.112: (+)-α-terpineol synthase EC 4.2.3.113: terpinolene synthase EC 4.2.3.114: γ-terpinene synthase EC 4.2.3.115: α-terpinene synthase EC 4.2.3.116: (+)-camphene synthase EC 4.2.3.117: (–)-camphene synthase EC 4.2.3.118: 2-methylisoborneol synthase EC 4.2.3.119: (-)-α-pinene synthase EC 4.2.3.120: (-)-β-pinene synthase EC 4.2.3.121: (+)-α-pinene synthase EC 4.2.3.122: (+)-β-pinene synthase EC 4.2.3.123: β-sesquiphellandrene synthase EC 4.2.3.124: 2-deoxy-scyllo-inosose synthase EC 4.2.3.125: α-muurolene synthase EC 4.2.3.126: γ-muurolene synthase EC 4.2.3.127: β-copaene synthase EC 4.2.3.128: β-cubebene synthase EC 4.2.3.129:
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
(+)-sativene synthase EC 4.2.3.130: tetraprenyl-β-curcumene synthase EC 4.2.3.131: miltiradiene synthase EC 4.2.3.132: neoabietadiene synthase EC 4.2.3.133: α-copaene synthase EC 4.2.3.134: 5-phosphooxy-L-lysine phospho-lyase EC 4.2.3.135: Δ6-protoilludene synthase EC 4.2.3.136: α-isocomene synthase EC 4.2.3.137: (E)-2-epi-β-caryophyllene synthase EC 4.2.3.138: (+)-epi-α-bisabolol synthase EC 4.2.3.139: valerena-4,7(11)-diene synthase EC 4.2.3.140: cis-abienol synthase Enzymes from EC 4.2.3.141 on have no Wikipedia articles EC 4.2.3.141: sclareol synthase EC 4.2.3.142: 7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] EC 4.2.3.143: kunzeaol synthase EC 4.2.3.144: geranyllinalool synthase EC 4.2.3.145: ophiobolin F synthase EC 4.2.3.146: cyclooctat-9-en-7-ol synthase EC 4.2.3.147: pimaradiene synthase EC 4.2.3.148: cembrene C synthase EC 4.2.3.149: nephthenol synthase EC 4.2.3.150: cembrene A synthase EC 4.2.3.151: pentamethylcyclopentadecatrienol synthase EC 4.2.3.152: 2-epi-5-epi-valiolone synthase EC 4.2.3.153: (5-formylfuran-3-yl)methyl phosphate synthase EC 4.2.3.154: demethyl-4-deoxygadusol synthase EC 4.2.3.155: 2-epi-valiolone synthase EC 4.2.3.156: hydroxysqualene synthase EC 4.2.3.157: (+)-isoafricanol synthase EC 4.2.3.158: (–)-spiroviolene synthase EC 4.2.3.159: tsukubadiene synthase EC 4.2.3.160: (2S,3R,6S,9S)-(–)-protoillud-7-ene synthase EC 4.2.3.161: (3S)-(+)-asterisca-2(9),6-diene synthase EC 4.2.3.162: (–)-α-amorphene synthase EC 4.2.3.163: (+)-corvol ether B synthase EC 4.2.3.164: (+)-eremophilene synthase EC 4.2.3.165: (1R,4R,5S)-(–)-guaia-6,10(14)-diene synthase EC 4.2.3.166: (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol synthase EC 4.2.3.167: dolabella-3,7-dien-18-ol synthase EC 4.2.3.168: dolathalia-3,7,11-triene synthase EC 4.2.3.169: 7-epi-α-eudesmol synthase EC 4.2.3.170: 4-epi-cubebol synthase EC 4.2.3.171: (+)-corvol ether A synthase EC 4.2.3.172: 10-epi-juneol synthase EC 4.2.3.173: τ-cadinol synthase EC 4.2.3.174: (2E,6E)-hedycaryol synthase EC 4.2.3.175: 10-epi-cubebol synthase EC 4.2.3.176: sesterfisherol synthase EC 4.2.3.177: β-thujene synthase EC 4.2.3.178: stellata-2,6,19-triene synthase EC 4.2.3.179: guaia-4,6-diene synthase EC 4.2.3.180: pseudolaratriene synthase EC 4.2.3.181: selina-4(15),7(11)-diene synthase EC 4.2.3.182: pristinol synthase EC 4.2.3.183: nezukol synthase EC 4.2.3.184: 5-hydroxy-α-gurjunene synthase EC 4.2.3.185: ent-atiserene synthase EC 4.2.3.186: ent-13-epi-manoyl oxide synthase EC 4.2.3.187: (2Z,6E)-hedycaryol synthase EC 4.2.3.188: β-geranylfarnesene synthase EC 4.2.3.189: 9,13-epoxylabd-14-ene synthase EC 4.2.3.190: manoyl oxide synthase EC 4.2.3.191: cycloaraneosene synthase EC 4.2.3.192: labda-7,13(16),14-triene synthase EC 4.2.3.193: (12E)-labda-8(17),12,14-triene synthase EC 4.2.3.194: (–)-drimenol synthase EC 4.2.3.195: rhizathalene A synthase EC 4.2.3.196: dolabradiene synthase EC 4.2.3.197: eudesmane-5,11-diol synthase EC 4.2.3.198: α-selinene
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
synthase EC 4.2.3.199: (–)-5-epieremophilene synthase EC 4.2.3.200: β-pinacene synthase EC 4.2.3.201: hydropyrene synthase EC 4.2.3.202: hydropyrenol synthase EC 4.2.3.203: isoelisabethatriene synthase EC 4.2.3.204: valerianol synthase EC 4.2.3.205: sodorifen synthase === EC 4.2.99: Other Carbon-Oxygen Lyases === EC 4.2.99.1: Now EC 4.2.2.1, hyaluronate lyase EC 4.2.99.2: Now EC 4.2.3.1, threonine synthase EC 4.2.99.3: Now EC 4.2.2.2, pectate lyase EC 4.2.99.4: Now EC 4.2.2.3, poly(β-D-mannuronate) lyase EC 4.2.99.5: deleted EC 4.2.99.6: Now included with EC 4.2.2.4 (chondroitin ABC lyase) and EC 4.2.2.5 (chondroitin AC lyase) EC 4.2.99.7: Now EC 4.2.3.2, ethanolamine-phosphate phospho-lyase EC 4.2.99.8: Now EC 2.5.1.47, cysteine synthase EC 4.2.99.9: Now EC 2.5.1.48, cystathionine γ-synthase EC 4.2.99.10: Now EC 2.5.1.49 EC 2.5.1.49, O-acetylhomoserine aminocarboxypropyltransferase EC 4.2.99.11: Now EC 4.2.3.3, methylglyoxal synthase EC 4.2.99.12: carboxymethyloxysuccinate lyase EC 4.2.99.13: Now EC 2.5.1.50, zeatin 9-aminocarboxyethyltransferase EC 4.2.99.14: Now EC 2.5.1.51, β-pyrazolylalanine synthase EC 4.2.99.15: Now EC 2.5.1.52, L-mimosine synthase EC 4.2.99.16: Now EC 2.5.1.53, uracilylalanine synthase EC 4.2.99.17: Listed as EC 2.5.1.51, β-pyrazolylalanine synthase EC 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase EC 4.2.99.19: Now EC 4.4.1.23, 2-hydroxypropyl-CoM lyase EC 4.2.99.20: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase EC 4.2.99.21: isochorismate lyase EC 4.2.99.22: tuliposide A-converting enzyme * EC 4.2.99.23: tuliposide B-converting enzyme * EC 4.2.99.24: thebaine synthase * *No Wikipedia article == EC 4.3: Carbon-Nitrogen Lyases == === EC 4.3.1: Ammonia-Lyases === EC 4.3.1.1: aspartate ammonia-lyase EC 4.3.1.2: methylaspartate ammonia-lyase EC 4.3.1.3: histidine ammonia-lyase EC 4.3.1.4: formiminotetrahydrofolate cyclodeaminase EC 4.3.1.5: Now divided into EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase) EC 4.3.1.6: β-alanyl-CoA ammonia-lyase EC 4.3.1.7: ethanolamine ammonia-lyase EC 4.3.1.8: Now EC 2.5.1.61, hydroxymethylbilane synthase EC 4.3.1.9: glucosaminate ammonia-lyase EC 4.3.1.10: serine-sulfate ammonia-lyase EC 4.3.1.11: Deleted: inadequately characterized EC 4.3.1.12: ornithine cyclodeaminase EC 4.3.1.13: carbamoyl-serine ammonia-lyase EC 4.3.1.14: 3-aminobutyryl-CoA ammonia-lyase EC 4.3.1.15: diaminopropionate ammonia-lyase EC 4.3.1.16: threo-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.17: L-serine ammonia-lyase EC
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
4.3.1.18: D-serine ammonia-lyase EC 4.3.1.19: threonine ammonia-lyase EC 4.3.1.20: erythro-3-hydroxy-L-aspartate ammonia-lyase EC 4.3.1.21: identical to EC 4.3.1.9, glucosaminate ammonia-lyase EC 4.3.1.22: 3,4-dihydroxyphenylalanine reductive deaminase EC 4.3.1.23: tyrosine ammonia-lyase EC 4.3.1.24: phenylalanine ammonia-lyase EC 4.3.1.25: phenylalanine/tyrosine ammonia-lyase EC 4.3.1.26: Now EC 1.21.3.9, dichlorochromopyrrolate synthase EC 4.3.1.27: threo-3-hydroxy-D-aspartate ammonia-lyase EC 4.3.1.28: L-lysine cyclodeaminase EC 4.3.1.29: D-glucosaminate-6-phosphate ammonia-lyase * EC 4.3.1.30: dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase * EC 4.3.1.31: L-tryptophan ammonia lyase * EC 4.3.1.32: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase * *No Wikipedia article === EC 4.3.2: Amidine-Lyases === EC 4.3.2.1: argininosuccinate lyase EC 4.3.2.2: adenylosuccinate lyase EC 4.3.2.3: ureidoglycolate lyase EC 4.3.2.4: purine imidazole-ring cyclase EC 4.3.2.5: peptidylamidoglycolate lyase EC 4.3.2.6: γ-L-glutamyl-butirosin B γ-glutamyl cyclotransferase EC 4.3.2.7: glutathione-specific γ-glutamylcyclotransferase * EC 4.3.2.8: γ-glutamylamine cyclotransferase * EC 4.3.2.9: γ-glutamylcyclotransferase * EC 4.3.2.10: imidazole glycerol-phosphate synthase * *No Wikipedia article === EC 4.3.3: Amine-Lyases === EC 4.3.3.1: 3-ketovalidoxylamine C-N-lyase EC 4.3.3.2: strictosidine synthase EC 4.3.3.3: deacetylisoipecoside synthase EC 4.3.3.4: deacetylipecoside synthase EC 4.3.3.5: 4′-demethylrebeccamycin synthase EC 4.3.3.6: pyridoxal 5′-phosphate synthase (glutamine hydrolysing) EC 4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase === EC 4.3.99: Other Carbon-Nitrogen Lyases === EC 4.3.99.1: Now EC 4.2.1.104, cyanate hydratase EC 4.3.99.2: Now EC 7.2.4.1, carboxybiotin decarboxylase EC 4.3.99.3: 7-carboxy-7-deazaguanine synthase EC 4.3.99.4: choline trimethylamine-lyase * *No Wikipedia article == EC 4.4: Carbon-Sulfur Lyases == === EC 4.4.1: Carbon-sulfur lyases (only sub-subclass identified to date) === EC 4.4.1.1: cystathionine γ-lyase EC 4.4.1.2: homocysteine desulfhydrase EC 4.4.1.3: dimethylpropiothetin dethiomethylase EC 4.4.1.4: alliin lyase EC 4.4.1.5: lactoylglutathione lyase EC 4.4.1.6: Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase EC 4.4.1.7: Now included with EC 2.5.1.18 glutathione transferase EC 4.4.1.8: Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase EC 4.4.1.9: L-3-cyanoalanine synthase EC 4.4.1.10: cysteine lyase EC 4.4.1.11: methionine γ-lyase EC 4.4.1.12: deleted: activity due to EC 2.3.3.15, sulfoacetaldehyde acetyltransferase EC 4.4.1.13: cysteine-S-conjugate β-lyase EC 4.4.1.14: 1-aminocyclopropane-1-carboxylate synthase EC 4.4.1.15: D-cysteine desulfhydrase EC 4.4.1.16: selenocysteine
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
lyase EC 4.4.1.17: holocytochrome-c synthase EC 4.4.1.18: Now EC 1.8.3.5, prenylcysteine oxidase EC 4.4.1.19: phosphosulfolactate synthase EC 4.4.1.20: leukotriene-C4 synthase EC 4.4.1.21: S-ribosylhomocysteine lyase EC 4.4.1.22: S-(hydroxymethyl)glutathione synthase EC 4.4.1.23: 2-hydroxypropyl-CoM lyase EC 4.4.1.24: (2R)-sulfolactate sulfo-lyase EC 4.4.1.25: L-cysteate sulfo-lyase EC 4.4.1.26: olivetolic acid cyclase EC 4.4.1.27: Now EC 3.13.1.5, carbon disulfide hydrolase *No Wikipedia article == EC 4.5: Carbon-Halide Lyases == === EC 4.5.1: Carbon-halide lyases (only sub-subclass identified to date) === EC 4.5.1.1: DDT-dehydrochlorinase EC 4.5.1.2: 3-chloro-D-alanine dehydrochlorinase EC 4.5.1.3: dichloromethane dehalogenase EC 4.5.1.4: L-2-amino-4-chloropent-4-enoate dehydrochlorinase EC 4.5.1.5: S-carboxymethylcysteine synthase == EC 4.6: Phosphorus-Oxygen Lyases == === EC 4.6.1: Phosphorus-oxygen lyases (only sub-subclass identified to date) === EC 4.6.1.1: adenylate cyclase EC 4.6.1.2: guanylate cyclase EC 4.6.1.3: Now EC 4.2.3.4, 3-dehydroquinate synthase EC 4.6.1.4: Now EC 4.2.3.5, chorismate synthase EC 4.6.1.5: Now EC 4.2.3.7, pentalenene synthase EC 4.6.1.6: cytidylate cyclase EC 4.6.1.7: Now EC 4.2.3.8, casbene synthase EC 4.6.1.8: Now EC 4.2.3.10, (-)-endo-fenchol synthase EC 4.6.1.9: Now Now EC 4.2.3.11, sabinene-hydrate synthase EC 4.6.1.10: Now EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase EC 4.6.1.11: Now EC 4.2.3.13, (+)-δ-cadinene synthase EC 4.6.1.12: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase EC 4.6.1.13: phosphatidylinositol diacylglycerol-lyase EC 4.6.1.14: glycosylphosphatidylinositol diacylglycerol-lyase EC 4.6.1.15: FAD-AMP lyase (cyclizing) EC 4.6.1.16: tRNA-intron lyase EC 4.6.1.17: cyclic pyranopterin monophosphate synthase * EC 4.6.1.18: pancreatic ribonuclease * EC 4.6.1.19: ribonuclease T2 * EC 4.6.1.20: ribonuclease U2 * EC 4.6.1.21: Enterobacter ribonuclease * EC 4.6.1.22: Bacillus subtilis ribonuclease * EC 4.6.1.23: ribotoxin * EC 4.6.1.24: ribonuclease T1 * EC 4.6.1.25: bacteriophage T4 restriction endoribonuclease RegB * *No Wikipedia article == EC 4.7: Carbon-phosphorus lyases == === EC 4.7.1: Carbon-phosphorus lyases (only sub-subclass identified to date) === EC 4.7.1.1 α-D ribose 1-methylphosphonate 5-phosphate C-P-lyase * *No Wikipedia article == EC 4.8: Nitrogen-oxygen lyases == === EC 4.8.1: Hydro-lyases === EC 4.8.1.1: L-piperazate synthase * EC 4.8.1.2: aliphatic
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
aldoxime dehydratase * EC 4.8.1.3: indoleacetaldoxime dehydratase * EC 4.8.1.4: phenylacetaldoxime dehydratase * *No Wikipedia article == EC 4.98: ATP-independent chelatases == === EC 4.98.1: Forming coordination complexes === EC 4.98.1.1: protoporphyrin ferrochelatase == EC 4.99: Other Lyases == === EC 4.99.1: Sole sub-subclass for lyases that do not belong in the other subclasses === EC 4.99.1.1: Now EC 4.98.1.1 EC 4.99.1.2: alkylmercury lyase EC 4.99.1.3: sirohydrochlorin cobaltochelatase EC 4.99.1.4: sirohydrochlorin ferrochelatase EC 4.99.1.5: Now EC 4.8.1.2, aliphatic aldoxime dehydratase EC 4.99.1.6: Now EC 4.8.1.3, indoleacetaldoxime dehydratase EC 4.99.1.7: Now EC 4.8.1.4, phenylacetaldoxime dehydratase EC 4.99.1.8: heme ligase EC 4.99.1.9:: coproporphyrin ferrochelatase * EC 4.99.1.10: magnesium dechelatase * EC 4.99.1.11: sirohydrochlorin nickelchelatase * EC 4.99.1.12: pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase * *No Wikipedia article == References ==
|
{
"page_id": 5506837,
"source": null,
"title": "List of EC numbers (EC 4)"
}
|
The study of electromagnetism in higher education, as a fundamental part of both physics and electrical engineering, is typically accompanied by textbooks devoted to the subject. The American Physical Society and the American Association of Physics Teachers recommend a full year of graduate study in electromagnetism for all physics graduate students. A joint task force by those organizations in 2006 found that in 76 of the 80 US physics departments surveyed, a course using John Jackson's Classical Electrodynamics was required for all first year graduate students. For undergraduates, there are several widely used textbooks, including David Griffiths' Introduction to Electrodynamics and Electricity and Magnetism by Edward Purcell and David Morin. Also at an undergraduate level, Richard Feynman's classic Lectures on Physics is available online to read for free. == Physics == === Undergraduate (introductory and intermediate) === There are several widely used undergraduate textbooks in electromagnetism, including David Griffiths' Introduction to Electrodynamics as well as Electricity and Magnetism by Edward Purcell and David Morin. Richard Feynman's Lectures on Physics also include a volume on electromagnetism that is available to read online for free, through the California Institute of Technology. In addition, there are popular physics textbooks that include electricity and magnetism among the material they cover, such as David Halliday and Robert Resnick's Fundamentals of Physics. Feynman RP, Leighton RB, Sands M, Electromagnetism and Matter, Basic Books, 2010. Grant IS, Phillips WR, Electromagnetism, 2nd ed, Wiley, 1990. Griffiths DJ, Introduction to Electrodynamics, 5th ed, Cambridge University, 2024. Halliday D, Resnick R, Walker J, Fundamentals of Physics, Extended 12th ed, Wiley, 2022. Heald MA, Marion JB, Classical Electromagnetic Radiation, 3rd ed, Dover, 2012. Müller-Kirsten HJW, Electrodynamics, 2nd ed, World Scientific, 2011. Ohanian HC, Classical Electrodynamics, 2nd ed, Jones & Bartlett, 2006. Pauli W, Electrodynamics, Dover, 2000. Pollack GL, Stump DR, Electromagnetism,
|
{
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
}
|
Addison-Wesley, 2002. Purcell EM, Morin DJ, Electricity and Magnetism, 3rd ed, Cambridge University, 2013. Reitz JR, Milford FJ, Christy RW, Foundations of Electromagnetic Theory, 4th ed, Pearson, 2009. Saslow W, Electricity Magnetism and Light, Academic, 2002. Schwartz M, Principles of Electrodynamics, Dover, 1987. Tamm IE, Fundamentals of the Theory of Electricity, Mir, 9th ed, 1979. Wangsness RK, Electromagnetic Fields, 2nd ed, Wiley, 1986. === Graduate === A 2006 report by a joint taskforce between the American Physical Society and the American Association of Physics Teachers found that 76 of the 80 physics departments surveyed require a first-year graduate course in John Jackson's Classical Electrodynamics. This made Jackson's book the most popular textbook in any field of graduate-level physics, with Herbert Goldstein's Classical Mechanics as the second most popular with adoption at 48 universities. James Russ, professor of physics at Carnegie Mellon University, claims Jackson's textbook has been "[t]he classic electrodynamics text for the past four decades" and that it is "the book from which most current-generation physicists took their first course." In addition to Jackson's textbook there are other classic textbooks like Classical Electricity and Magnetism by Pief Panofsky and Melba Phillips, and Electrodynamics of Continuous Media by Lev Landau, Evgeny Lifshitz, and Lev Pitaevskii, both pre-dating Jackson's book. Among the textbooks published after Jackson's book, Julian Schwinger's 1970s lecture notes is a mentionable book first published in 1998 posthumously. Due to the domination of Jackson's textbook in graduate physics education, even physicists like Schwinger became frustrated competing with Jackson and because of this, the publication of Schwinger's book was postponed so that it was finally completed and published by his colleagues. In addition to the mentioned classic books, in recent years there have been a few well-received electromagnetic textbooks published for graduate studies in physics, with one of the
|
{
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
}
|
most notable being Modern Electrodynamics by Andrew Zangwill published in 2013, which has been praised by many physicists like John Joannopoulos, Michael Berry, Rob Phillips, Alain Aspect, Roberto Merlin, Shirley Chiang, Roy Schwitters but also well received in the electrical engineering community. Another notable textbook is Classical Electromagnetism in a Nutshell by Anupam Garg published in 2012, which has been also praised by physicists like Anthony Zee, Ramamurti Shankar, Jainendra Jain, John Belcher. Here is the list of some important textbooks that discuss generic physical areas of electromagnetism. Brau CA, Modern Problems in Classical Electrodynamics, Oxford University, 2004. Chaichian M, Merches I, Radu D, Tureanu A, Electrodynamics: An Intensive Course, Springer, 2016. Di Bartolo B, Classical Theory of Electromagnetism, 3rd ed, World Scientific, 2018. Franklin J, Classical Electromagnetism, 2nd ed, Dover, 2017. Freeman R, King J, Lafyatis G, Electromagnetic Radiation, Oxford University, 2019. Garg A, Classical Electromagnetism in a Nutshell, Princeton University, 2012. Good RH, Nelson TJ, Classical Theory of Electric and Magnetic Fields, Academic, 1971. Jackson JD, Classical Electrodynamics, 3rd ed, Wiley, 1999. Jentschura UD, Advanced Classical Electrodynamics: Green Functions, Regularizations, Multipole Decompositions, World Scientific, 2017. Landau LD, Lifshitz EM, Pitaevskii LP, Electrodynamics of Continuous Media, 2nd ed, Pergamon, 1984. Maggiore M, A Modern Introduction to Classical Electrodynamics, Oxford University, 2023. Melia F, Electrodynamics, University of Chicago, 2001. Milton KA, Schwinger J, Classical Electrodynamics, 2nd ed, CRC, 2024. Panofsky WKH, Phillips M, Classical Electricity and Magnetism, 2nd ed, Dover, 2005. Sommerfeld A, Electrodynamics, Academic, 1952. Wald RM, Advanced Classical Electromagnetism, Princeton University, 2022. Wilcox W, Thron C, Macroscopic Electrodynamics: An Introductory Graduate Treatment, 2nd ed, World Scientific, 2024. Zangwill A, Modern Electrodynamics, Cambridge University, 2013. === Specialized === Here is the list of some important graduate textbooks that discuss particular physical areas of electromagnetism. Barut AO, Electrodynamics and Classical
|
{
"page_id": 39323412,
"source": null,
"title": "List of textbooks in electromagnetism"
}
|
Theory of Fields and Particles, Dover, 1980. Baylis WE, Electrodynamics: A Modern Geometric Approach, Birkhäuser, 1999. Böttcher CJF, Bordewijk P, Van Belle OC, Rip A, Theory of Electric Polarization, 2nd ed, 2 vols, Elsevier, 1973, 1978. Clemmow PC, Dougherty JP, Electrodynamics of Particles and Plasmas, CRC, 2018. Cullity DB, Stock SR, Elements of X-Ray Diffraction, 3rd ed, Pearson, 2014. Eringen AC, Maugin GA, Electrodynamics of Continua, 2 vols, Springer, 1990. Ginzburg VL, The Propagation of Electromagnetic Waves in Plasmas, 2nd ed, Pergamon, 1970. Hehl FW, Obukhov YN, Foundations of Classical Electrodynamics: Charge, Flux, and Metric, Springer, 2003. Landau LD, Lifshitz EM, The Classical Theory of Fields, 4th ed, Pergamon, 1975. Lechner K, Classical Electrodynamics: A Modern Perspective, Springer, 2018. Oppenheimer JR, Lectures on Electrodynamics, Gordon & Breach, 1970. Post EJ, Formal Structure of Electromagnetics: General Covariance and Electromagnetics, Dover, 1997. Rohrlich F, Classical Charged Particles, 3rd ed, World Scientific, 2007. Rybicki GB, Lightman AP, Radiative Processes in Astrophysics, Wiley, 1979. There is a controversy in scientific community about using different units in electromagnetism that have been discussed. == Electrical engineering == According to a 2011 review of analytical and computational textbooks in electromagnetism by David Davidson, Julius Stratton's Electromagnetic Theory remains the classic text in electromagnetism and is still regularly cited. Davidson goes on to point out that Constantine Balanis' Advanced Engineering Electromagnetics and Roger Harrington's Time-Harmonic Electromagnetic Fields are standard references at the post-graduate level. Also for advanced undergraduate level, the textbook Fields and Waves in Communication Electronics by Simon Ramo, John Whinnery, and Theodore Van Duzer is considered as standard reference. Traditional differences between a physicist's point of view and an electrical engineer's point of view in studying electromagnetism have been noted. According to a 2023 lecture titled What Physicists Don't Know About Electromagnetism given by the theoretical
|
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physicist Hans Schantz and based on the comparison of textbooks Electromagnetic Theory by Julius Stratton and Classical Electrodynamics by John Jackson, Schantz argues "today's physicists who are educated using curriculum out of Jackson are less informed about practical electromagnetics than their counterparts of 80 years ago," and says it's because physicists are now shifted from classical electrodynamics to quantum electrodynamics. Schantz also continues that concepts like impedance, Smith chart, antenna, and electromagnetic energy flow, are not appreciated by physicists. Mathematician Sergei Schelkunoff who made many contributions to engineering electromagnetism also noted differences between physicist's and electrical engineer's view in electromagnetism. According to Schelkunoff: The classical physicist, being concerned largely with isolated transmission systems, has emphasized only one wave concept, that of the velocity of propagation or more generally of the propagation constant. But the communication engineer who is interested in "chains" of such systems from the very start is forced to adopt a more general attitude and introduce the second important wave concept, that of the impedance. The physicist concentrates his attention on one particular wave: a wave of force, or a wave of velocity or a wave of displacement. His original differential equations may be of the first order and may involve both force and velocity; but by tradition he eliminates one of these variables, obtains a second order differential equation in the other and calls it the "wave equation." Thus he loses sight of the interdependence of force and velocity waves and he does not stress the difference which may exist between waves in different media even though the velocity of wave propagation is the same. The engineer, on the other hand, thinks in terms of the original "pair of wave equations" and keeps constantly in mind this interdependence between force and velocity waves. The usefulness of electrical
|
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"page_id": 39323412,
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engineering's approach to electromagnetic problems has also been noted by other physicists like Robert Dicke and more specially Julian Schwinger. Schwinger's emphasis on using electrical engineering's point of view was even more general than just in electromagnetic phenomena so that he argued for the use of engineering worldview even in pure branches of physics like high-energy physics. Schwinger also said about his transformation from a person who saw electrical engineering problems as a pure physicist to a person who saw pure physical problems as an electrical engineer: "I first approached radar problems as a nuclear physicist; soon I began to think of nuclear physics in the language of electrical engineering." Many of the important and classic graduate electromagnetic textbooks related to electrical engineering listed here are published or reissued by IEEE under the name of The IEEE Press Series on Electromagnetic Wave Theory. === Undergraduate (introductory and intermediate) === Cheng DK, Field and Wave Electromagnetics, 2nd ed, Addison-Wesley, 1989. Hammond P, Electromagnetism for Engineers: An Introductory Course, 4th ed, Oxford University, 1997. Haus HA, Melcher JR, Electromagnetic Fields and Energy, Prentice Hall, 1989. Hayt WH, Buck JA, Engineering Electromagnetics, 9th ed, McGraw Hill, 2018. Ida N, Engineering Electromagnetics, 4th ed, Springer, 2021. Johnk CTA, Engineering Electromagnetic Fields and Waves, 2nd ed, Wiley, 1991. Jordan EC, Balmain KG, Electromagnetic Waves and Radiating Systems, 2nd ed, Prentice Hall, 1968. Kraus JD, Fleisch DA, Russ SH, Electromagnetics with Applications, 5th ed, McGraw Hill, 1999. Lorrain P, Corson DR, Lorrain F, Electromagnetic Fields and Waves: Including Electric Circuits, 3rd ed, WH Freeman, 1988. Ramo S, Whinnery JR, Van Duzer T, Fields and Waves in Communication Electronics, 3rd ed, Wiley, 1994. Sadiku MNO, Elements of Electromagnetics, 7th ed, Oxford University, 2018. Strangeway RA, Holland SS, Richie JE, Electromagnetics and Transmission Lines: Essentials for Electrical Engineering,
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"page_id": 39323412,
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2nd ed, Wiley, 2022. Ulaby FT, Ravaioli U, Fundamentals of Applied Electromagnetics, 8th ed, Pearson, 2020. === Graduate === Balanis CA, Advanced Engineering Electromagnetics, 3rd ed, Wiley, 2024. Chew WC, Waves and Fields in Inhomogeneous Media, IEEE, 1995. Collin RE, Field Theory of Guided Waves, 2nd ed, Wiley-IEEE, 1991. Felsen LB, Marcuvitz N, Radiation and Scattering of Waves, Wiley-IEEE, 2003. Harrington RF, Time-Harmonic Electromagnetic Fields, Wiley-IEEE, 2001. Ishimaru A, Electromagnetic Wave Propagation, Radiation, and Scattering: From Fundamentals to Applications, 2nd ed, Wiley-IEEE, 2017. Jones DS, The Theory of Electromagnetism, Pergamon, 1964. Kong JA, Electromagnetic Wave Theory, 3rd ed, EMW, 2008. Schelkunoff SA, Electromagnetic Waves, Van Nostrand, 1943. Smythe WR, Static and Dynamic Electricity, 3rd ed, Hemisphere, 1989. Stratton JA, Electromagnetic Theory, Wiley-IEEE, 2007. Van Bladel J, Electromagnetic Fields, 2nd ed, Wiley-IEEE, 2007. === Specialized === Beckmann P, Spizzichino A, The Scattering of Electromagnetic Waves from Rough Surfaces, Artech House, 1987. Dudley DG, Mathematical Foundations for Electromagnetic Theory, Wiley-IEEE, 1994. Hanson GW, Yakovlev AB, Operator Theory for Electromagnetics: An Introduction, Springer, 2002. Idemen MM, Discontinuities in the Electromagnetic Field, Wiley-IEEE, 2011. Ishimaru A, Wave Propagation and Scattering in Random Media, IEEE-Oxford University, 1997. Kazimierczuk MK, High-Frequency Magnetic Components, 2nd ed, Wiley, 2014. Lindell IV, Methods for Electromagnetic Field Analysis, 2nd ed, Wiley-IEEE, 1996. McNamara DA, Pistotius CWI, Malherbe JAG, Introduction to Uniform Geometrical Theory of Diffraction, Artech House, 1990. Mittra R, Lee SW, Analytical Techniques in the Theory of Guided Waves, Macmillan, 1971. Senior TBA, Volakis JL, Approximate Boundary Conditions in Electromagnetics, IEE 1995. Tai CT, Dyadic Green Functions in Electromagnetic Theory, 2nd ed, IEEE, 1994. Tsang L, Kong JA, Ding KH, Ao CO, Scattering of Electromagnetic Waves, 3 vols, Wiley, 2001. Ufimtsev PY, Fundamentals of the Physical Theory of Diffraction, 2nd ed, Wiley-IEEE, 2014. Van Bladel J, Singular Electromagnetic Fields
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"page_id": 39323412,
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and Sources, Wiley-IEEE, 1991. Wait JR, Electromagnetic Waves in Stratified Media, 2nd ed, IEEE-Oxford University, 1996. === Radio-frequency === Balanis CA, Antenna Theory: Analysis and Design, 4th ed, Wiley, 2016. Collin RE, Foundations for Microwave Engineering, 2nd ed, Wiley-IEEE, 2001. Elliott RS, Antenna Theory and Design, Wiley-IEEE, 2003. Garg R, Bhartia P, Bahl I, Ittipiboon A, Microstrip Antenna Design Handbook, Artech House, 2001. Kraus JD, Marhefka RJ, Khan AS, Antennas and Wave Propagation, 5th ed, McGraw Hill, 2017. Marcuvitz N, Waveguide Handbook, IET, 2009. Milligan TA, Modern Antenna Design, 2nd ed, Wiley-IEEE 2005. Paul CR, Scully RC, Steffka MA, Introduction to Electromagnetic Compatibility, 3rd ed, Wiley, 2023. Pozar DM, Microwave Engineering, 4th ed, Wiley, 2012. Rizzi PA, Microwave Engineering: Passive Circuits, Prentice Hall, 1988. Ruck GT, Barrick DE, Stuart WD, Krichbaum CK, Radar Cross Section Handbook, 2 vols, Kluwer-Plenum, 1970. Stutzman WL, Thiele GA, Antenna Theory and Design, 3rd ed, Wiley, 2013. Tsang L, Kong JA, Shin RT, Theory of Microwave Remote Sensing, Wiley, 1985. Ulaby FT, Moore RK, Fung AK, Microwave Remote Sensing: Active and Passive, 3 vols, Artech House, 1981, 1982, 1986. === Metamaterials === Caloz C, Itoh T, Electromagnetic Metamaterials: Transmission Line Theory and Microwave Applications (The Engineering Approach), Wiley-IEEE, 2006. Capolino F, (Ed), Metamaterials Handbook, 2 vols, CRC, 2009. Cui TJ, Smith DR, Liu R, (Eds), Metamaterials: Theory, Design, and Applications, Springer, 2010. Eleftheriades GV, Balmain KG, (Eds), Negative-Refraction Metamaterials: Fundamental Principles and Applications, Wiley-IEEE, 2005. Engheta N, Ziolkowski RW, (Eds), Metamaterials: Physics and Engineering Explorations, Wiley-IEEE, 2006. Marqués R, Martín F, Sorolla M, Metamaterials with Negative Parameters: Theory, Design, and Microwave Applications, Wiley, 2008. Munk BA, Frequency Selective Surfaces: Theory and Design, Wiley, 2000. Munk BA, Metamaterials: Critique and Alternatives, Wiley, 2009. Ramakrishna SA, Grzegorczyk TM, Physics and Applications of Negative Refractive Index Materials, CRC,
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"page_id": 39323412,
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2008. Sarychev AK, Shalaev VM, Electrodynamics of Metamaterials, World Scientific, 2007. Tretyakov S, Analytical Modeling in Applied Electromagnetics, Artech House, 2003. Yang F, Rahmat-Samii Y, Electromagnetic Band Gap Structures in Antenna Engineering, Cambridge University, 2009. === Computational === Booton RC, Computational Methods for Electromagnetics and Microwaves, Wiley, 1992. Chew WC, Jin JM, Michielssen E, Song J, (Eds), Fast and Efficient Algorithms in Computational Electromagnetics, Artech House, 2001. Gibson WC, The Method of Moments in Electromagnetics, 3rd ed, CRC, 2022. Harrington RF, Field Computation by Moment Methods, Wiley-IEEE, 2000. Itoh T, (Ed), Numerical Techniques for Microwave and Millimeter-Wave Passive Structures, Wiley, 1989. Jin JM, The Finite Element Method in Electromagnetics, 3rd ed, Wiley-IEEE, 2014. Jones DS, Methods in Electromagnetic Wave Propagation, 2nd ed, Wiley-IEEE, 1994. Kunz KS, Luebbers RJ, The Finite Difference Time Domain Method for Electromagnetics, CRC, 1993. Peterson AF, Ray SL, Mittra R, Computational Methods for Electromagnetics, Wiley-IEEE, 1997. Sadiku MNO, Computational Electromagnetics with MATLAB, 4th ed, CRC, 2019. Silvester PP, Ferrari RL, Finite Elements for Electrical Engineers, 3rd ed, Cambridge University, 1996. Taflove A, Hagness SC, (Eds), Computational Electrodynamics: The Finite-Difference Time-Domain Method, 3rd ed, Artech House, 2005. == Optics == There are also many outstanding and notable textbooks published in optics which is a branch of electromagnetism dealing with interactions of light or visible spectrum electromagnetism with matter. Here is the list of some important textbooks in different areas of classical optics. These textbooks are suitable for both physics and electrical engineering studies depending on the context. === Generic === Born M, Wolf E, Principles of Optics, 7th ed, Cambridge University, 2019. Fowles GR, Introduction to Modern Optics, 2nd ed, Dover, 1989. Guenther BD, Modern Optics, 2nd ed, Oxford University, 2015. Hecht E, Optics, 5th ed, Pearson, 2017. Iizuka K, Engineering Optics, 4th ed, Springer, 2019. Jenkins
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"page_id": 39323412,
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FA, White HE, Fundamentals of Optics, 4th ed, McGraw Hill, 2001. Lipson A, Lipson SG, Lipson H, Optical Physics, 4th ed, Cambridge University, 2010. Shiell R, McNab I, Pedrottis' Introduction to Optics, 4th ed, Cambridge University, 2024. Smith WJ, Modern Optical Engineering: The Design of Optical Systems, 4th ed, McGraw Hill, 2008. Sommerfeld A, Optics, Academic, 1954. === Specialized === Agrawal GP, Fiber-Optic Communication Systems, 5th ed, Wiley, 2021. Agrawal GP, Nonlinear Fiber Optics, 6th ed, Elsevier, 2019. Boyd RW, Nonlinear Optics, 4th ed, Elsevier, 2020. Goodman JW, Introduction to Fourier Optics, 4th ed, WH Freeman, 2017. Goodman JW, Statistical Optics, 2nd ed, Wiley, 2015. Haus HA, Waves and Fields in Optoelectronics, Prentice Hall, 1984. Luneburg RK, Mathematical Theory of Optics, University of California, 1964. Maier SA, Plasmonics: Fundamentals and Applications, Springer, 2007. Novotny L, Hecht B, Principles of Nano-Optics, 2nd ed, Cambridge University, 2012. Saleh BEA, Teich MC, Fundamentals of Photonics, 3rd ed, Wiley, 2019. Shen YR, Principles of Nonlinear Optics, Wiley, 1984. Yariv A, Yeh P, Photonics: Optical Electronics in Modern Communications, 6th ed, Oxford University, 2007. === Light scattering === Berne BJ, Pecora R, Dynamic Light Scattering: With Applications to Chemistry, Biology, and Physics, Dover, 2000. Bohren CF, Huffman DR, Absorption and Scattering of Light by Small Particles, Wiley, 2004. Kerker M, The Scattering of Light and Other Electromagnetic Radiation, Academic, 1969. Mishchenko MI, Travis LD, Lacis AA, Scattering, Absorption, and Emission of Light by Small Particles, NASA-Cambridge University, 2006. van de Hulst HC, Light Scattering by Small Particles, Dover, 1981. Yeh P, Optical Waves in Layered Media, Wiley, 1988. == Magnetism == Another branch of electromagnetism that has been developed separately is magnetism, which is about studying magnetic properties of different materials and their interactions with electromagnetic fields. There are also many classic textbooks published in
|
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"page_id": 39323412,
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magnetism which some of them are listed here and they could be used in both physics and electrical engineering studies depending on the context. Aharoni A, Introduction to the Theory of Ferromagnetism, 2nd ed, Oxford University, 1996. Blundell S, Magnetism in Condensed Matter, Oxford University, 2001. Bozorth RM, Ferromagnetism, Wiley-IEEE, 2003. Chikazumi S, Physics of Ferromagnetism, 2nd ed, Oxford University, 1997. Coey JMD, Magnetism and Magnetic Materials, Cambridge University, 2009. Cullity BD, Graham CD, Introduction to Magnetic Materials, 2nd ed, Wiley-IEEE, 2009. Dunlop DJ, Özdemir Ö, Rock Magnetism: Fundamentals and Frontiers, Cambridge University, 1997. Jiles D, Introduction to Magnetism and Magnetic Materials, 3rd ed, CRC, 2016. Krishnan KM, Fundamentals and Applications of Magnetic Materials, Oxford University, 2016. Morrish AH, The Physical Principles of Magnetism, Wiley-IEEE, 2001. O'handley RC, Modern Magnetic Materials: Principles and Applications, Wiley, 2000. Spaldin NA, Magnetic Materials: Fundamentals and Applications, 2nd ed, Cambridge University, 2010. == Magnetohydrodynamics == Magnetohydrodynamics is an interdisciplinary branch of physics that uses continuum mechanics to describe the interaction of electromagnetic fields with fluids that are conductive. It combines classical electromagnetism with fluid mechanics by combination of Maxwell equations with Navier-Stokes equations. This relatively new branch of physics was first developed by Hannes Alfvén in a 1942 paper published in Nature titled Existence of Electromagnetic-Hydrodynamic Waves. In 1950 Alfvén published a textbook titled Cosmical Electrodynamics which considered as the seminal work in the field of magnetohydrodynamics. There are also two closely related fields to the traditional field of magnetohydrodynamics which are called electrohydrodynamics and ferrohydrodynamics. Electrohydrodynamics deals with interaction of electromagnetic fields with weakly conductive fluids and ferrohydrodynamics deals with interaction of electromagnetic fields with magnetic fluids. Today magnetohydrodynamics and its related fields have many applications in plasma physics, electrical engineering, mechanical engineering, astrophysics, geophysics and many other scientific branches. Here is the
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"page_id": 39323412,
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list of some important textbooks in different areas of electro-magneto-ferro-hydrodynamics. Alfvén H, Fälthammar CG, Cosmical Electrodynamics: Fundamental Principles, 2nd ed, Oxford University, 1963. Biskamp D, Magnetohydrodynamic Turbulence, Cambridge University, 2003. Biskamp D, Nonlinear Magnetohydrodynamics, Cambridge University, 1993. Blums E, Cebers A, Maiorov MM, Magnetic Fluids, De Gruyter, 1996. Castellanos A, (Ed), Electrohydrodynamics, Springer, 1998. Cowling TG, Magnetohydrodynamics, 2nd ed, Adam Hilger, 1976. Davidson PA, Introduction to Magnetohydrodynamics, 2nd ed, Cambridge University, 2017. Moreau R, Magnetohydrodynamics, Springer, 1990. Priest E, Magnetohydrodynamics of the Sun, Cambridge University, 2014. Priest E, Forbes T, Magnetic Reconnection: MHD Theory and Applications, Cambridge University, 2000. Roberts PH, An Introduction to Magnetohydrodynamics, Elsevier, 1967. Rosensweig RE, Ferrohydrodynamics, Dover, 2014. Sutton GW, Sherman A, Engineering Magnetohydrodynamics, Dover, 2006. == Historical == There are many important books in electromagnetism which are generally considered as historical classics and some of them are listed here. Abraham M, Becker R, The Classical Theory of Electricity and Magnetism, 8th ed, Blackie & Son, 1932. Green G, An Essay on the Application of Mathematical Analysis to the Theories of Electricity and Magnetism, T Wheelhouse, 1828. Heaviside O, Electromagnetic Theory, 3rd ed, 3 vols, The Electrician, 1893, 1899, 1912. Hertz H, Electric Waves: Being Researches on the Propagation of Electric Action with Finite Velocity through Space, Macmillan, 1893. Jeans JH, The Mathematical Theory of Electricity and Magnetism, 5th ed, Cambridge University, 1927. Macdonald HM, Electric Waves, Cambridge University, 1902. Maxwell JC, A Treatise on Electricity and Magnetism, 3rd ed, 2 vols, Clarendon, 1891. Planck M, Theory of Electricity and Magnetism, 2nd ed, Macmillan, 1932. Schott GA, Electromagnetic Radiation and the Mechanical Reactions Arising from It, Cambridge University, 1912. Thomson JJ, Elements of the Mathematical Theory of Electricity and Magnetism, 4th ed, Cambridge University, 1909. Whittaker ET, A History of the Theories of Aether and Electricity,
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2nd ed, 2 vols, Thomas Nelson, 1951. == See also == == Notes == == References ==
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"page_id": 39323412,
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Ammonium polyphosphate is an inorganic salt of polyphosphoric acid and ammonia containing both chains and possibly branching. Its chemical formula is H(NH4PO3)nOH showing that each monomer consists of an orthophosphate radical of a phosphorus atom with three oxygens and one negative charge neutralized by an ammonium cation leaving two bonds free to polymerize. In the branched cases some monomers are missing the ammonium anion and instead link to three other monomers. The properties of ammonium polyphosphate depend on the number of monomers in each molecule and to a degree on how often it branches. Shorter chains (n < 100) are more water sensitive and less thermally stable than longer chains (n > 1000), but short polymer chains (e.g. pyro-, tripoly-, and tetrapoly-) are more soluble and show increasing solubility with increasing chain length. Ammonium polyphosphate can be prepared by reacting concentrated phosphoric acid with ammonia. However, iron and aluminum impurities, soluble in concentrated phosphoric acid, form gelatinous precipitates or "sludges" in ammonium polyphosphate at pH between 5 and 7. Other metal impurities such as copper, chromium, magnesium, and zinc form granular precipitates. However, depending on the degree of polymerization, ammonium polyphosphate can act as a chelating agent to keep certain metal ions dissolved in solution. Ammonium polyphosphate is used as a food additive, emulsifier, (E number: E545) and as a fertilizer. Ammonium polyphosphate (APP) is also used as a flame retardant in many applications such as paints and coatings, and in a variety of polymers: the most important ones are polyolefins, and particularly polypropylene, where APP is part of intumescent systems. Compounding with APP-based flame retardants in polypropylene is described in. Further applications are thermosets, where APP is used in unsaturated polyesters and gel coats (APP blends with synergists), epoxies and polyurethane castings (intumescent systems). APP is also applied to
|
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"page_id": 15664920,
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"title": "Ammonium polyphosphate"
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flame retard polyurethane foams. Ammonium polyphosphates used as flame retardants in polymers have long chains and a specific crystallinity (Form II). They start to decompose at 240 °C to form ammonia and phosphoric acid. The phosphoric acid acts as an acid catalyst in the dehydration of carbon-based poly-alcohols, such as cellulose in wood. The phosphoric acid reacts with alcohol groups to form heat-unstable phosphate esters. The esters decompose to release carbon dioxide and regenerate the phosphoric acid catalyst . In the gas phase, the release of non-flammable carbon dioxide helps to dilute the oxygen of the air and flammable decomposition products of the material that is burning. In the condensed phase, the resultant carbonaceous char helps to shield the underlying polymer from attack by oxygen and radiant heat. Use as an intumescent is achieved when combined with starch-based materials such as pentaerythritol and melamine as expanding agents. The mechanisms of intumescence and the mode of action of APP are described in a series of publications. == References == == External links == US 2950961, Striplin Jr., Marcus M.; Stinson, John M. & Potts, John M., "Production of liquid fertilizers", published 1960-08-30, assigned to Tennessee Valley Authority US 4211546, Jensen, William C., "Process for preparation of ammonium polyphosphate", published 1980-07-08, assigned to Western Farm Services Inc.
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This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. == EC 3.1: Acting on Ester Bonds == === EC 3.1.1: Carboxylic Ester Hydrolases === EC 3.1.1.1: carboxylesterase EC 3.1.1.2: arylesterase EC 3.1.1.3: triacylglycerol lipase EC 3.1.1.4: phospholipase A2 EC 3.1.1.5: lysophospholipase EC 3.1.1.6: acetylesterase EC 3.1.1.7: acetylcholinesterase EC 3.1.1.8: cholinesterase EC 3.1.1.9: deleted, a side reaction of EC 3.1.1.8 cholinesterase EC 3.1.1.10: tropinesterase EC 3.1.1.11: pectinesterase EC 3.1.1.12: deleted, identical with EC 3.1.1.1 carboxylesterase EC 3.1.1.13: sterol esterase EC 3.1.1.14: chlorophyllase EC 3.1.1.15: L-arabinonolactonase EC 3.1.1.16: deleted, mixture of EC 5.3.3.4 (muconolactone Δ-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase) EC 3.1.1.17: gluconolactonase EC 3.1.1.18: deleted, now included with EC 3.1.1.17 gluconolactonase EC 3.1.1.19: uronolactonase EC 3.1.1.20: tannase EC 3.1.1.21: deleted, now known to be catalysed by EC 3.1.1.1, carboxylesterase and EC 3.1.1.3, triacylglycerol lipase. EC 3.1.1.22: hydroxybutyrate-dimer hydrolase EC 3.1.1.23: acylglycerol lipase EC 3.1.1.24: 3-oxoadipate enol-lactonase EC 3.1.1.25: 1,4-lactonase EC 3.1.1.26: galactolipase EC 3.1.1.27: 4-pyridoxolactonase EC 3.1.1.28: acylcarnitine hydrolase EC 3.1.1.29: aminoacyl-tRNA hydrolase EC 3.1.1.30: D-arabinonolactonase EC 3.1.1.31: 6-phosphogluconolactonase EC 3.1.1.32: phospholipase A1 EC 3.1.1.33: 6-acetylglucose deacetylase EC 3.1.1.34: lipoprotein lipase EC 3.1.1.35: dihydrocoumarin hydrolase EC 3.1.1.36: limonin-D-ring-lactonase EC 3.1.1.37: steroid-lactonase EC 3.1.1.38: triacetate-lactonase EC 3.1.1.39: actinomycin lactonase EC 3.1.1.40: orsellinate-depside hydrolase EC 3.1.1.41: cephalosporin-C deacetylase EC 3.1.1.42: chlorogenate hydrolase EC 3.1.1.43: α-amino-acid esterase EC 3.1.1.44: 4-methyloxaloacetate esterase EC 3.1.1.45: carboxymethylenebutenolidase EC 3.1.1.46: deoxylimonate A-ring-lactonase EC 3.1.1.47: 1-alkyl-2-acetylglycerophosphocholine esterase EC 3.1.1.48: fusarinine-C ornithinesterase EC 3.1.1.49: sinapine esterase EC 3.1.1.50: wax-ester hydrolase EC 3.1.1.51: phorbol-diester hydrolase EC 3.1.1.52: phosphatidylinositol deacylase EC 3.1.1.53: sialate O-acetylesterase EC 3.1.1.54: acetoxybutynylbithiophene
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"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
deacetylase EC 3.1.1.55: acetylsalicylate deacetylase EC 3.1.1.56: methylumbelliferyl-acetate deacetylase EC 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase EC 3.1.1.58: N-acetylgalactosaminoglycan deacetylase EC 3.1.1.59: juvenile-hormone esterase EC 3.1.1.60: bis(2-ethylhexyl)phthalate esterase EC 3.1.1.61: protein-glutamate methylesterase EC 3.1.1.62: Now listed as EC 3.5.1.47, N-acetyldiaminopimelate deacetylase EC 3.1.1.63: 11-cis-retinyl-palmitate hydrolase EC 3.1.1.64: retinoid isomerohydrolase EC 3.1.1.65: L-rhamnono-1,4-lactonase EC 3.1.1.66: 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene deacetylase EC 3.1.1.67: fatty-acyl-ethyl-ester synthase EC 3.1.1.68: xylono-1,4-lactonase EC 3.1.1.69: Now EC 3.5.1.89, N-acetylglucosaminylphosphatidylinositol deacetylase EC 3.1.1.70: cetraxate benzylesterase EC 3.1.1.71: acetylalkylglycerol acetylhydrolase EC 3.1.1.72: acetylxylan esterase EC 3.1.1.73: feruloyl esterase EC 3.1.1.74: cutinase EC 3.1.1.75: poly(3-hydroxybutyrate) depolymerase EC 3.1.1.76: poly(3-hydroxyoctanoate) depolymerase EC 3.1.1.77: acyloxyacyl hydrolase EC 3.1.1.78: polyneuridine-aldehyde esterase EC 3.1.1.79: hormone-sensitive lipase EC 3.1.1.80: acetylajmaline esterase EC 3.1.1.81: quorum-quenching N-acyl-homoserine lactonase EC 3.1.1.82: pheophorbidase EC 3.1.1.83: monoterpene ε-lactone hydrolase EC 3.1.1.84: cocaine esterase EC 3.1.1.85: pimelyl-(acyl-carrier protein) methyl ester esterase EC 3.1.1.86: rhamnogalacturonan acetylesterase EC 3.1.1.87: fumonisin B1 esterase EC 3.1.1.88: pyrethroid hydrolase EC 3.1.1.89: protein phosphatase methylesterase-1 EC 3.1.1.90: all-trans-retinyl ester 13-cis isomerohydrolase EC 3.1.1.91: 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase EC 3.1.1.92: 4-sulfomuconolactone hydrolase EC 3.1.1.93: mycophenolic acid acyl-glucuronide esterase EC 3.1.1.94: versiconal hemiacetal acetate esterase * EC 3.1.1.95: aclacinomycin methylesterase * EC 3.1.1.96: D-aminoacyl-tRNA deacylase * EC 3.1.1.97: methylated diphthine methylhydrolase * EC 3.1.1.98: [Wnt protein] O-palmitoleoyl-L-serine hydrolase * EC 3.1.1.99: 6-deoxy-6-sulfogluconolactonase * EC 3.1.1.100: chlorophyllide a hydrolase * EC 3.1.1.101: poly(ethylene terephthalate) hydrolase * EC 3.1.1.102: mono(ethylene terephthalate) hydrolase * EC 3.1.1.103: teichoic acid D-alanine hydrolase * EC 3.1.1.104: 5-phospho-D-xylono-1,4-lactonase * EC 3.1.1.105: 3-O-acetylpapaveroxine carboxylesterase * EC 3.1.1.106: O-acetyl-ADP-ribose deacetylase * EC 3.1.1.107: apo-salmochelin esterase * EC 3.1.1.108: iron(III)-enterobactin esterase * EC 3.1.1.109: iron(III)-salmochelin esterase * EC 3.1.1.110: xylono-1,5-lactonase * EC 3.1.1.111: phosphatidylserine sn-1 acylhydrolase * EC 3.1.1.112: isoamyl acetate esterase * EC 3.1.1.113: ethyl acetate hydrolase * EC 3.1.1.114: methyl acetate hydrolase EC 3.1.1.115: D-apionolactonase * EC 3.1.1.116: sn-1-specific diacylglycerol lipase * EC 3.1.1.117: (4-O-methyl)-D-glucuronate—lignin
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
esterase * EC 3.1.1.118: phospholipid sn-1 acylhydrolase * *No Wikipedia article === EC 3.1.2: Thioester Hydrolases === EC 3.1.2.1: acetyl-CoA hydrolase EC 3.1.2.2: palmitoyl-CoA hydrolase EC 3.1.2.3: succinyl-CoA hydrolase EC 3.1.2.4: 3-hydroxyisobutyryl-CoA hydrolase EC 3.1.2.5: hydroxymethylglutaryl-CoA hydrolase EC 3.1.2.6: hydroxyacylglutathione hydrolase EC 3.1.2.7: glutathione thiolesterase EC 3.1.2.8: Now included with EC 3.1.2.6 hydroxyacylglutathione hydrolase EC 3.1.2.9: S-acetoacetylhydrolipoate hydrolase deleted EC 3.1.2.10: formyl-CoA hydrolase EC 3.1.2.11: acetoacetyl-CoA hydrolase EC 3.1.2.12: S-formylglutathione hydrolase EC 3.1.2.13: S-succinylglutathione hydrolase EC 3.1.2.14: oleoyl-[acyl-carrier-protein] hydrolase EC 3.1.2.15: covered by EC 3.4.19.12, ubiquitinyl hydrolase 1 EC 3.1.2.16: citrate lyase deacetylase EC 3.1.2.17: (S)-methylmalonyl-CoA hydrolase EC 3.1.2.18: ADP-dependent short-chain-acyl-CoA hydrolase EC 3.1.2.19: ADP-dependent medium-chain-acyl-CoA hydrolase EC 3.1.2.20: acyl-CoA hydrolase EC 3.1.2.21: dodecanoyl-(acyl-carrier-protein) hydrolase EC 3.1.2.22: palmitoyl[protein] hydrolase EC 3.1.2.23: 4-hydroxybenzoyl-CoA thioesterase EC 3.1.2.24: transferred entry now EC 3.13.1.3, 2′-hydroxybiphenyl-2-sulfinate desulfinase. EC 3.1.2.25: phenylacetyl-CoA hydrolase EC 3.1.2.26: Now EC 2.8.3.25, bile acid CoA transferase EC 3.1.2.27: choloyl-CoA hydrolase EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase EC 3.1.2.29: fluoroacetyl-CoA thioesterase EC 3.1.2.30: (3S)-malyl-CoA thioesterase * EC 3.1.2.31: dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase * EC 3.1.2.32: 2-aminobenzoylacetyl-CoA thioesterase * *No Wikipedia article === EC 3.1.3: Phosphoric Monoester Hydrolases === EC 3.1.3.1: alkaline phosphatase EC 3.1.3.2: acid phosphatase EC 3.1.3.3: phosphoserine phosphatase EC 3.1.3.4: phosphatidate phosphatase EC 3.1.3.5: 5′-nucleotidase EC 3.1.3.6: 3′-nucleotidase EC 3.1.3.7: 3′(2′),5′-bisphosphate nucleotidase EC 3.1.3.8: 3-phytase EC 3.1.3.9: glucose-6-phosphatase EC 3.1.3.10: glucose-1-phosphatase EC 3.1.3.11: fructose-bisphosphatase EC 3.1.3.12: trehalose-phosphatase EC 3.1.3.13: Recent studies have shown that this is a partial activity of EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) EC 3.1.3.14: methylphosphothioglycerate phosphatase EC 3.1.3.15: histidinol-phosphatase EC 3.1.3.16: protein serine/threonine phosphatase EC 3.1.3.17: (phosphorylase) phosphatase EC 3.1.3.18: phosphoglycolate phosphatase EC 3.1.3.19: glycerol-2-phosphatase EC 3.1.3.20: phosphoglycerate phosphatase EC 3.1.3.21: glycerol-1-phosphatase EC 3.1.3.22: mannitol-1-phosphatase EC 3.1.3.23: sugar-phosphatase EC 3.1.3.24: sucrose-phosphatase EC 3.1.3.25: inositol-phosphate phosphatase EC 3.1.3.26: 4-phytase EC 3.1.3.27: phosphatidylglycerophosphatase EC 3.1.3.28: ADP-phosphoglycerate phosphatase EC 3.1.3.29: N-acylneuraminate-9-phosphatase
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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EC 3.1.3.30: The activity may be that of an acid phosphatase EC 3.1.3.31: The activity may be that of an acid phosphatase EC 3.1.3.32: polynucleotide 3′-phosphatase EC 3.1.3.33: polynucleotide 5′-phosphatase EC 3.1.3.34: deoxynucleotide 3′-phosphatase EC 3.1.3.35: thymidylate 5′-phosphatase EC 3.1.3.36: phosphoinositide 5-phosphatase EC 3.1.3.37: sedoheptulose-bisphosphatase EC 3.1.3.38: 3-phosphoglycerate phosphatase EC 3.1.3.39: streptomycin-6-phosphatase EC 3.1.3.40: guanidinodeoxy-scyllo-inositol-4-phosphatase EC 3.1.3.41: 4-nitrophenylphosphatase EC 3.1.3.42: glycogen-synthase-D] phosphatase EC 3.1.3.43: [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase EC 3.1.3.44: [acetyl-CoA carboxylase]-phosphatase EC 3.1.3.45: 3-deoxy-manno-octulosonate-8-phosphatase EC 3.1.3.46: fructose-2,6-bisphosphate 2-phosphatase EC 3.1.3.47: [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase EC 3.1.3.48: protein-tyrosine-phosphatase EC 3.1.3.49: [pyruvate kinase]-phosphatase EC 3.1.3.50: sorbitol-6-phosphatase EC 3.1.3.51: dolichyl-phosphatase EC 3.1.3.52: [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase EC 3.1.3.53: [myosin-light-chain] phosphatase EC 3.1.3.54: fructose-2,6-bisphosphate 6-phosphatase EC 3.1.3.55: caldesmon-phosphatase EC 3.1.3.56: inositol-polyphosphate 5-phosphatase EC 3.1.3.57: inositol-1,4-bisphosphate 1-phosphatase EC 3.1.3.58: sugar-terminal-phosphatase EC 3.1.3.59: alkylacetylglycerophosphatase EC 3.1.3.60: phosphoenolpyruvate phosphatase EC 3.1.3.61: deleted, as its existence has not been established EC 3.1.3.62: multiple inositol-polyphosphate phosphatase EC 3.1.3.63: 2-carboxy-D-arabinitol-1-phosphatase EC 3.1.3.64: phosphatidylinositol-3-phosphatase EC 3.1.3.65: Now included with EC 3.1.3.64, phosphatidylinositol-3-phosphatase EC 3.1.3.66: phosphatidylinositol-3,4-bisphosphate 4-phosphatase EC 3.1.3.67: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase EC 3.1.3.68: 2-deoxyglucose-6-phosphatase EC 3.1.3.69: glucosylglycerol 3-phosphatase EC 3.1.3.70: mannosyl-3-phosphoglycerate phosphatase EC 3.1.3.71: 2-phosphosulfolactate phosphatase EC 3.1.3.72: 5-phytase EC 3.1.3.73: adenosylcobalamin/α-ribazole phosphatase EC 3.1.3.74: pyridoxal phosphatase EC 3.1.3.75: phosphoethanolamine/phosphocholine phosphatase EC 3.1.3.76: lipid-phosphate phosphatase EC 3.1.3.77: acireductone synthase EC 3.1.3.78: phosphatidylinositol-4,5-bisphosphate 4-phosphatase EC 3.1.3.79: mannosylfructose-phosphate phosphatase EC 3.1.3.80: 2,3-bisphosphoglycerate 3-phosphatase EC 3.1.3.81: Transferred entry, now EC 3.6.1.75, diacylglycerol diphosphate phosphatase EC 3.1.3.82: D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase EC 3.1.3.83: D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase EC 3.1.3.84: ADP-ribose 1′′-phosphate phosphatase EC 3.1.3.85: glucosyl-3-phosphoglycerate phosphatase EC 3.1.3.86: phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase EC 3.1.3.87: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase EC 3.1.3.88: 5′′-phosphoribostamycin phosphatase * No Wikipedia article === EC 3.1.4: Phosphoric Diester Hydrolases === EC 3.1.4.1: phosphodiesterase I EC 3.1.4.2: glycerophosphocholine phosphodiesterase EC 3.1.4.3: lecithinase C EC 3.1.4.4: phospholipase D EC 3.1.4.5: Now EC 3.1.21.1, deoxyribonuclease I EC 3.1.4.6: Now EC 3.1.22.1, deoxyribonuclease II EC
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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3.1.4.7: Now EC 3.1.31.1, micrococcal nuclease EC 3.1.4.8: Now EC 3.1.27.3, ribonuclease T1 EC 3.1.4.9: Now EC 3.1.30.2, Serratia marcescens nuclease EC 3.1.4.10: Now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase EC 3.1.4.11: phosphoinositide phospholipase C EC 3.1.4.12: sphingomyelin phosphodiesterase EC 3.1.4.13: serine-ethanolaminephosphate phosphodiesterase EC 3.1.4.14: [acyl-carrier-protein] phosphodiesterase EC 3.1.4.15 : transferred to EC 2.7.7.89, adenylyl-[glutamateammonia ligase] phosphorylase EC 3.1.4.16: 2′,3′-cyclic-nucleotide 2′-phosphodiesterase EC 3.1.4.17: 3′,5′-cyclic-nucleotide phosphodiesterase EC 3.1.4.18: Now EC 3.1.16.1, spleen exonuclease EC 3.1.4.19: Now EC 3.1.13.3, oligonucleotidase EC 3.1.4.20: Now EC 3.1.13.1, exoribonuclease II EC 3.1.4.21: Now EC 3.1.30.1, Aspergillus nuclease S1 EC 3.1.4.22: Now EC 3.1.27.5, pancreatic ribonuclease EC 3.1.4.23: Now EC 3.1.27.1, ribonuclease T2 EC 3.1.4.24: deleted EC 3.1.4.25: Now EC 3.1.11.1, exodeoxyribonuclease I EC 3.1.4.26: deleted EC 3.1.4.27: Now EC 3.1.11.2, exodeoxyribonuclease III EC 3.1.4.28: Now EC 3.1.11.3, exodeoxyribonuclease (lambda-induced) EC 3.1.4.29: deleted EC 3.1.4.30: Now EC 3.1.21.2, deoxyribonuclease IV (phage-T4-induced) EC 3.1.4.31: Now EC 3.1.11.4 EC 3.1.4.32: deleted EC 3.1.4.33: deleted EC 3.1.4.34: deleted EC 3.1.4.35: 3′,5′-cyclic-GMP phosphodiesterase EC 3.1.4.36: Now with EC 3.1.4.43 EC 3.1.4.37: 2′,3′-cyclic-nucleotide 3'-phosphodiesterase EC 3.1.4.38: glycerophosphocholine cholinephosphodiesterase EC 3.1.4.39: alkylglycerophosphoethanolamine phosphodiesterase EC 3.1.4.40: CMP-N-acylneuraminate phosphodiesterase EC 3.1.4.41: sphingomyelin phosphodiesterase D EC 3.1.4.42: glycerol-1,2-cyclic-phosphate 2-phosphodiesterase EC 3.1.4.43: glycerophosphoinositol inositolphosphodiesterase EC 3.1.4.44: glycerophosphoinositol glycerophosphodiesterase EC 3.1.4.45: N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase EC 3.1.4.46: glycerophosphodiester phosphodiesterase EC 3.1.4.47: Now EC 4.6.1.14, glycosylphosphatidylinositol diacylglycerol-lyase EC 3.1.4.48: dolichylphosphate-glucose phosphodiesterase EC 3.1.4.49: dolichylphosphate-mannose phosphodiesterase EC 3.1.4.50: glycosylphosphatidylinositol phospholipase D EC 3.1.4.51: glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase EC 3.1.4.52: cyclic-guanylate-specific phosphodiesterase EC 3.1.4.53: 3′,5′-cyclic-AMP phosphodiesterase EC 3.1.4.54: N-acetylphosphatidylethanolamine-hydrolysing phospholipase D EC 3.1.4.55: phosphoribosyl 1,2-cyclic phosphate phosphodiesterase * EC 3.1.4.56: 7,8-dihydroneopterin 2′,3′-cyclic phosphate phosphodiesterase EC 3.1.4.57: phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase EC 3.1.4.58: RNA 2′,3′-cyclic 3′-phosphodiesterase * EC 3.1.4.59: cyclic-di-AMP phosphodiesterase * EC 3.1.4.60: pApA phosphodiesterase * EC 3.1.4.61: cyclic 2,3-diphosphoglycerate hydrolase * *No Wikipedia article === EC 3.1.5: Triphosphoric Monoester Hydrolases === EC 3.1.5.1: dGTPase ===
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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EC 3.1.6: Sulfuric Ester Hydrolases === EC 3.1.6.1: arylsulfatase (type I) EC 3.1.6.2: steryl-sulfatase EC 3.1.6.3: glycosulfatase EC 3.1.6.4: N-acetylgalactosamine-6-sulfatase EC 3.1.6.5: deleted EC 3.1.6.6: choline-sulfatase EC 3.1.6.7: cellulose-polysulfatase EC 3.1.6.8: cerebroside-sulfatase EC 3.1.6.9: chondro-4-sulfatase EC 3.1.6.10: chondro-6-sulfatase EC 3.1.6.11: disulfoglucosamine-6-sulfatase EC 3.1.6.12: N-acetylgalactosamine-6-sulfatase EC 3.1.6.13: iduronate-2-sulfatase EC 3.1.6.14: N-acetylglucosamine-6-sulfatase EC 3.1.6.15: N-sulfoglucosamine-3-sulfatase EC 3.1.6.16: monomethyl-sulfatase EC 3.1.6.17: D-lactate-2-sulfatase EC 3.1.6.18: Glucuronate-2-sulfatase EC 3.1.6.19: (R)-specific secondary-alkylsulfatase (type III) * EC 3.1.6.20: S-sulfosulfanyl-L-cysteine sulfohydrolase * EC 3.1.6.21: linear primary-alkylsulfatase * EC 3.1.6.22: branched primary-alkylsulfatase * *No Wikipedia article === EC 3.1.7: Diphosphoric Monoester Hydrolases === EC 3.1.7.1: prenyl-diphosphatase EC 3.1.7.2: guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase EC 3.1.7.3: monoterpenyl-diphosphatase EC 3.1.7.4: Now recognized as two enzymes EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141, sclareol synthase EC 3.1.7.5: geranylgeranyl diphosphate diphosphatase EC 3.1.7.6: farnesyl diphosphatase EC 3.1.7.7: Now EC 4.2.3.194, (–)-drimenol synthase EC 3.1.7.8: Now known to be a partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase. EC 3.1.7.9: Now known to be a partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase EC 3.1.7.10: (13E)-labda-7,13-dien-15-ol synthase EC 3.1.7.11: geranyl diphosphate diphosphatase EC 3.1.7.12: (+)-kolavelool synthase * *No Wikipedia article === EC 3.1.8: Phosphoric Triester Hydrolases === EC 3.1.8.1: aryldialkylphosphatase EC 3.1.8.2: diisopropyl-fluorophosphatase === EC 3.1.11: Exodeoxyribonucleases Producing 5'-Phosphomonoesters === EC 3.1.11.1: exodeoxyribonuclease I EC 3.1.11.2: exodeoxyribonuclease III EC 3.1.11.3: exodeoxyribonuclease (lambda-induced) EC 3.1.11.4: exodeoxyribonuclease (phage SP3-induced) EC 3.1.11.5: exodeoxyribonuclease V EC 3.1.11.6: exodeoxyribonuclease VII EC 3.1.11.7: Now EC 3.6.1.71, adenosine-5′-diphospho-5′-[DNA] diphosphatase EC 3.1.11.8: Now EC 3.6.1.70, guanosine-5′-diphospho-5′-[DNA] diphosphatase === EC 3.1.13: Exoribonucleases Producing 5'-Phosphomonoesters === EC 3.1.13.1: exoribonuclease II EC 3.1.13.2: exoribonuclease H EC 3.1.13.3: oligonucleotidase EC 3.1.13.4: poly(A)-specific ribonuclease EC 3.1.13.5: ribonuclease D === EC 3.1.14: Exoribonucleases Producing 3'-Phosphomonoesters === EC 3.1.14.1: yeast ribonuclease === EC 3.1.15: Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters === EC 3.1.15.1: venom exonuclease === EC 3.1.16:
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters === EC 3.1.16.1: spleen exonuclease === EC 3.1.21: Endodeoxyribonucleases Producing 5'-Phosphomonoesters === EC 3.1.21.1: deoxyribonuclease I EC 3.1.21.2: deoxyribonuclease IV EC 3.1.21.3: type I site-specific deoxyribonuclease EC 3.1.21.4: type II site-specific deoxyribonuclease EC 3.1.21.5: type III site-specific deoxyribonuclease EC 3.1.21.6: CC-preferring endodeoxyribonuclease EC 3.1.21.7: deoxyribonuclease V EC 3.1.21.8: T4 deoxyribonuclease II * EC 3.1.21.9: T4 deoxyribonuclease IV * EC 3.1.21.10: crossover junction endodeoxyribonuclease * *No Wikipedia article === EC 3.1.22: Endodeoxyribonucleases Producing 3'-Phosphomonoesters === EC 3.1.22.1: deoxyribonuclease II EC 3.1.22.2: Aspergillus deoxyribonuclease K1 EC 3.1.22.3: now EC 3.1.21.7 EC 3.1.22.4: crossover junction endodeoxyribonuclease EC 3.1.22.5: deoxyribonuclease X === EC 3.1.23: and EC 3.1.24 now EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5 === Deleted sub-subclasses. === EC 3.1.25: Site-Specific Endodeoxyribonucleases Specific for Altered Bases === EC 3.1.25.1: deoxyribonuclease (pyrimidine dimer) EC 3.1.25.2: Now EC 4.2.99.18, DNA-(apurinic or apyrimidinic site) lyase === EC 3.1.26: Endoribonucleases Producing 5'-Phosphomonoesters === EC 3.1.26.1: Physarum polycephalum ribonuclease EC 3.1.26.2: ribonuclease α EC 3.1.26.3: ribonuclease III EC 3.1.26.4: ribonuclease H EC 3.1.26.5: ribonuclease P EC 3.1.26.6: ribonuclease IV EC 3.1.26.7: ribonuclease P4 EC 3.1.26.8: ribonuclease M5 EC 3.1.26.9: ribonuclease (poly-(U)-specific) EC 3.1.26.10: ribonuclease IX EC 3.1.26.11: tRNase Z EC 3.1.26.12: ribonuclease E EC 3.1.26.13: retroviral ribonuclease H === EC 3.1.27: Endoribonucleases Producing 3'-Phosphomonoesters === EC 3.1.27.1: Now EC 4.6.1.19, ribonuclease T2, since the primary reaction is that of a lyase EC 3.1.27.2: Now EC 4.6.1.22, Bacillus subtilis ribonuclease, since the reaction catalysed is that of a lyase EC 3.1.27.3: Now EC 4.6.1.24, ribonuclease T1, since the primary reaction is that of a lyase EC 3.1.27.4: Now EC 4.6.1.20, ribonuclease U2, since the primary reaction is that of a lyase EC 3.1.27.5: Now EC 4.6.1.18, pancreatic ribonuclease. EC 3.1.27.6: Now EC 4.6.1.21, Enterobacter ribonuclease, since the primary
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
reaction is that of a lyase EC 3.1.27.7: ribonuclease F EC 3.1.27.8: ribonuclease V EC 3.1.27.9: Now EC 4.6.1.16, tRNA-intron lyase EC 3.1.27.10: Now EC 4.6.1.23, ribotoxin, === EC 3.1.30: Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters === EC 3.1.30.1: Aspergillus nuclease S1 EC 3.1.30.2: Serratia marcescens nuclease === EC 3.1.31: Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters === EC 3.1.31.1: micrococcal nuclease == EC 3.2: Glycosylases == === EC 3.2.1: Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds === EC 3.2.1.1: α-amylase EC 3.2.1.2: β-amylase EC 3.2.1.3: glucan 1,4-α-glucosidase EC 3.2.1.4: cellulase EC 3.2.1.5: deleted EC 3.2.1.6: endo-1,3(4)-β-glucanase EC 3.2.1.7: inulinase EC 3.2.1.8: endo-1,4-β-xylanase EC 3.2.1.9: deleted EC 3.2.1.10: oligo-1,6-glucosidase EC 3.2.1.11: dextranase EC 3.2.1.12: Now included with EC 3.2.1.54, cyclomaltodextrinase EC 3.2.1.13: Now included with EC 3.2.1.54, cyclomaltodextrinase EC 3.2.1.14: chitinase EC 3.2.1.15: polygalacturonase EC 3.2.1.16: deleted EC 3.2.1.17: lysozyme EC 3.2.1.18: exo-α-sialidase EC 3.2.1.19: deleted EC 3.2.1.20: α-glucosidase EC 3.2.1.21: β-glucosidase EC 3.2.1.22: α-galactosidase EC 3.2.1.23: β-galactosidase EC 3.2.1.24: α-mannosidase EC 3.2.1.25: β-mannosidase EC 3.2.1.26: β-fructofuranosidase (invertase) EC 3.2.1.27: deleted EC 3.2.1.28: α,α-trehalase EC 3.2.1.29: Now included with EC 3.2.1.52, β-N-acetylhexosaminidase EC 3.2.1.30: Now included with EC 3.2.1.52, β-N-acetylhexosaminidase EC 3.2.1.31: β-glucuronidase EC 3.2.1.32: endo-1,3-β-xylanase EC 3.2.1.33: amylo-α-1,6-glucosidase EC 3.2.1.34: Now included with EC 3.2.1.35, hyaluronoglucosaminidase EC 3.2.1.35: hyaluronoglucosaminidase EC 3.2.1.36: hyaluronoglucuronidase EC 3.2.1.37: xylan 1,4-β-xylosidase EC 3.2.1.38: β-D-fucosidase EC 3.2.1.39: glucan endo-1,3-β-D-glucosidase EC 3.2.1.40: α-L-rhamnosidase EC 3.2.1.41: pullulanase EC 3.2.1.42: GDP-glucosidase EC 3.2.1.43: β-L-rhamnosidase EC 3.2.1.44: Now EC 3.2.1.211, endo-(13)-fucoidanase and EC 3.2.1.212, endo-(14)-fucoidanase EC 3.2.1.45: glucosylceramidase EC 3.2.1.46: galactosylceramidase EC 3.2.1.47: Now known to be catalyzed by EC 3.2.1.22, α-galactosidase EC 3.2.1.48: sucrose α-glucosidase EC 3.2.1.49: α-N-acetylgalactosaminidase EC 3.2.1.50: α-N-acetylglucosaminidase EC 3.2.1.51: α-L-fucosidase EC 3.2.1.52: β-N-acetylhexosaminidase EC 3.2.1.53: β-N-acetylgalactosaminidase EC 3.2.1.54: cyclomaltodextrinase EC 3.2.1.55: non-reducing end α-L-arabinofuranosidase
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
EC 3.2.1.56: glucuronosyl-disulfoglucosamine glucuronidase EC 3.2.1.57: isopullulanase EC 3.2.1.58: glucan 1,3-β-glucosidase EC 3.2.1.59: glucan endo-1,3-α-glucosidase EC 3.2.1.60: glucan 1,4-α-maltotetraohydrolase EC 3.2.1.61: mycodextranase EC 3.2.1.62: glycosylceramidase EC 3.2.1.63: 1,2-α-L-fucosidase EC 3.2.1.64: 2,6-β-fructan 6-levanbiohydrolase EC 3.2.1.65: levanase EC 3.2.1.66: Deleted entry: The activity is covered by EC 3.2.1.40, α-L-rhamnosidase EC 3.2.1.67: galacturan 1,4-α-galacturonidase EC 3.2.1.68: isoamylase EC 3.2.1.69: Now included with EC 3.2.1.41, pullulanase EC 3.2.1.70: glucan 1,6-α-glucosidase EC 3.2.1.71: glucan endo-1,2-β-glucosidase EC 3.2.1.72: xylan 1,3-β-xylosidase EC 3.2.1.73: licheninase EC 3.2.1.74: glucan 1,4-β-glucosidase EC 3.2.1.75: glucan endo-1,6-β-glucosidase EC 3.2.1.76: L-iduronidase EC 3.2.1.77: mannan 1,2-(1,3)-α-mannosidase EC 3.2.1.78: mannan endo-1,4-β-mannosidase EC 3.2.1.79: Now included with EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase EC 3.2.1.80: fructan β-fructosidase EC 3.2.1.81: β-agarase EC 3.2.1.82: exo-poly-α-digalacturonosidas EC 3.2.1.83: κ-carrageenase EC 3.2.1.84: glucan 1,3-α-glucosidase EC 3.2.1.85: 6-phospho-β-galactosidase EC 3.2.1.86: 6-phospho-β-glucosidase EC 3.2.1.87: capsular-polysaccharide endo-1,3-α-galactosidase EC 3.2.1.88: non-reducing end β-L-arabinopyranosidase EC 3.2.1.89: arabinogalactan endo-β-1,4-galactanase EC 3.2.1.90: Deleted, not sufficiently characterised. EC 3.2.1.91: cellulose 1,4-β-cellobiosidase (non-reducing end) EC 3.2.1.92: peptidoglycan β-N-acetylmuramidase EC 3.2.1.93: α,α-phosphotrehalase EC 3.2.1.94: glucan 1,6-α-isomaltosidase EC 3.2.1.95: dextran 1,6-α-isomaltotriosidase EC 3.2.1.96: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase EC 3.2.1.97: endo-α-N-acetylgalactosaminidase EC 3.2.1.98: glucan 1,4-α-maltohexaosidase EC 3.2.1.99: arabinan endo-1,5-α-L-arabinanase EC 3.2.1.100: mannan 1,4-mannobiosidase EC 3.2.1.101: mannan endo-1,6-α-mannosidase EC 3.2.1.102: blood-group-substance endo-1,4-β-galactosidase EC 3.2.1.103: keratan-sulfate endo-1,4-β-galactosidase EC 3.2.1.104: steryl-β-glucosidase EC 3.2.1.105: 3α(S)-strictosidine β-glucosidase EC 3.2.1.106: mannosyl-oligosaccharide glucosidase EC 3.2.1.107: protein-glucosylgalactosylhydroxylysine glucosidase EC 3.2.1.108: lactase EC 3.2.1.109: endogalactosaminidase EC 3.2.1.110: identical to EC 3.2.1.97, endo-α-N-acetylgalactosaminidase EC 3.2.1.111: 1,3-α-L-fucosidase EC 3.2.1.112: 2-deoxyglucosidase EC 3.2.1.113: mannosyl-oligosaccharide 1,2-α-mannosidase EC 3.2.1.114: mannosyl-oligosaccharide 1,3-1,6-α-mannosidas EC 3.2.1.115: branched-dextran exo-1,2-α-glucosidase EC 3.2.1.116: glucan 1,4-α-maltotriohydrolase EC 3.2.1.117: amygdalin β-glucosidase EC 3.2.1.118: prunasin β-glucosidase EC 3.2.1.119: vicianin β-glucosidase EC 3.2.1.120: oligoxyloglucan β-glycosidase EC 3.2.1.121: polymannuronate hydrolase EC 3.2.1.122: maltose-6′-phosphate glucosidase EC 3.2.1.123: endoglycosylceramidase EC 3.2.1.124: 3-deoxy-2-octulosonidase EC 3.2.1.125: raucaffricine β-glucosidase EC 3.2.1.126: coniferin β-glucosidase EC 3.2.1.127: 1,6-α-L-fucosidase EC 3.2.1.128: glycyrrhizin hydrolase EC 3.2.1.129: endo-α-sialidase EC 3.2.1.130:
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
glycoprotein endo-α-1,2-mannosidase EC 3.2.1.131: xylan α-1,2-glucuronosidase EC 3.2.1.132: chitosanase EC 3.2.1.133: glucan 1,4-α-maltohydrolase EC 3.2.1.134: difructose-anhydride synthase EC 3.2.1.135: neopullulanase EC 3.2.1.136: glucuronoarabinoxylan endo-1,4-β-xylanase EC 3.2.1.137: mannan exo-1,2-1,6-α-mannosidase EC 3.2.1.138: Now EC 4.2.2.15, anhydrosialidase EC 3.2.1.139: α-glucuronidase EC 3.2.1.140: lacto-N-biosidase EC 3.2.1.141: 4-α-D-{(1→4)-α-D-glucano}trehalose trehalohydrolase EC 3.2.1.142: limit dextrinase EC 3.2.1.143: poly(ADP-ribose) glycohydrolase EC 3.2.1.144: 3-deoxyoctulosonase EC 3.2.1.145: galactan 1,3-β-galactosidase EC 3.2.1.146: β-galactofuranosidase EC 3.2.1.147: thioglucosidase EC 3.2.1.148: The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase EC 3.2.1.149: β-primeverosidase EC 3.2.1.150: oligoxyloglucan reducing-end-specific cellobiohydrolase EC 3.2.1.151: xyloglucan-specific endo-β-1,4-glucanase EC 3.2.1.152: mannosylglycoprotein endo-β-mannosidase EC 3.2.1.153: fructan β-(2,1)-fructosidase EC 3.2.1.154: fructan β-(2,6)-fructosidase EC 3.2.1.155: xyloglucan-specific endo-processive β-1,4-glucanase EC 3.2.1.156: oligosaccharide reducing-end xylanase EC 3.2.1.157: ι-carrageenase EC 3.2.1.158: α-agarase EC 3.2.1.159: α-neoagaro-oligosaccharide hydrolase EC 3.2.1.160: identical to EC 3.2.1.155, xyloglucan-specific exo-β-1,4-glucanase EC 3.2.1.161: β-apiosyl-β-glucosidase EC 3.2.1.162: λ-carrageenase EC 3.2.1.163: 1,6-α-D-mannosidase EC 3.2.1.164: galactan endo-1,6-β-galactosidase EC 3.2.1.165: exo-1,4-β-D-glucosaminidase EC 3.2.1.166: heparanase EC 3.2.1.167: baicalin-β-D-glucuronidase EC 3.2.1.168: hesperidin 6-O-α-L-rhamnosyl-β-D-glucosidase EC 3.2.1.169: protein O-GlcNAcas EC 3.2.1.170: mannosylglycerate hydrolase EC 3.2.1.171: rhamnogalacturonan hydrolase EC 3.2.1.172: unsaturated rhamnogalacturonyl hydrolase EC 3.2.1.173: rhamnogalacturonan galacturonohydrolase EC 3.2.1.174: rhamnogalacturonan rhamnohydrolase EC 3.2.1.175: β-D-glucopyranosyl abscisate β-glucosidase EC 3.2.1.176: cellulose 1,4-β-cellobiosidase (reducing end) EC 3.2.1.177: α-D-xyloside xylohydrolase EC 3.2.1.178: β-porphyranase EC 3.2.1.179: gellan tetrasaccharide unsaturated glucuronyl hydrolase EC 3.2.1.180: unsaturated chondroitin disaccharide hydrolase EC 3.2.1.181: galactan endo-β-1,3-galactanase EC 3.2.1.182: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase EC 3.2.1.183: UDP-N-acetylglucosamine 2-epimerase (hydrolysing) EC 3.2.1.184: UDP-N,N′-diacetylbacillosamine 2-epimerase (hydrolysing) EC 3.2.1.185: non-reducing end β-L-arabinofuranosidase * EC 3.2.1.186: protodioscin 26-O-β-D-glucosidase * EC 3.2.1.187: (Ara-f)3-Hyp β-L-arabinobiosidase * EC 3.2.1.188: avenacosidase * EC 3.2.1.189: dioscin glycosidase (diosgenin-forming) * EC 3.2.1.190: dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming) * EC 3.2.1.191: ginsenosidase type III * EC 3.2.1.192: ginsenoside Rb1 β-glucosidase * EC 3.2.1.193: ginsenosidase type I * EC 3.2.1.194: ginsenosidase type IV * EC 3.2.1.195: 20-O-multi-glycoside ginsenosidase * EC 3.2.1.196: limit dextrin α-1,6-maltotetraose-hydrolase * EC 3.2.1.197:
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
β-1,2-mannosidase * EC 3.2.1.198: α-mannan endo-1,2-α-mannanase * EC 3.2.1.199: sulfoquinovosidase * EC 3.2.1.200: exo-chitinase (non-reducing end) * EC 3.2.1.201: exo-chitinase (reducing end) * EC 3.2.1.202: endo-chitodextinase * EC 3.2.1.203: carboxymethylcellulase * EC 3.2.1.204: 1,3-α-isomaltosidase * EC 3.2.1.205: isomaltose glucohydrolase * EC 3.2.1.206: oleuropein β-glucosidase * EC 3.2.1.207: mannosyl-oligosaccharide α-1,3-glucosidase * EC 3.2.1.208: glucosylglycerate hydrolase * EC 3.2.1.209: endoplasmic reticulum Man9GlcNAc2 1,2-α-mannosidase * EC 3.2.1.210: endoplasmic reticulum Man8GlcNAc2 1,2-α-mannosidase * EC 3.2.1.211: endo-(1→3)-fucoidanase * EC 3.2.1.212: endo-(1→4)-fucoidanase * EC 3.2.1.213: galactan exo-1,6-β-galactobiohydrolase (non-reducing end) * EC 3.2.1.214: exo β-1,2-glucooligosaccharide sophorohydrolase (non-reducing end) * *No Wikipedia article === EC 3.2.2: Hydrolysing N-Glycosyl Compounds === EC 3.2.2.1: purine nucleosidase EC 3.2.2.2: inosine nucleosidase EC 3.2.2.3: uridine nucleosidase EC 3.2.2.4: AMP nucleosidase EC 3.2.2.5: NAD+ glycohydrolase EC 3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase EC 3.2.2.7: adenosine nucleosidase EC 3.2.2.8: ribosylpyrimidine nucleosidase EC 3.2.2.9: adenosylhomocysteine nucleosidase EC 3.2.2.10: pyrimidine-5′-nucleotide nucleosidase EC 3.2.2.11: β-aspartyl-N-acetylglucosaminidase EC 3.2.2.12: inosinate nucleosidase EC 3.2.2.13: 1-methyladenosine nucleosidase EC 3.2.2.14: NMN nucleosidase EC 3.2.2.15: DNA-deoxyinosine glycosylase EC 3.2.2.16: methylthioadenosine nucleosidase EC 3.2.2.17: deoxyribodipyrimidine endonucleosidase EC 3.2.2.18: Now included with EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase EC 3.2.2.19: ADP-ribosylarginine hydrolase EC 3.2.2.20: DNA-3-methyladenine glycosylase I EC 3.2.2.21: DNA-3-methyladenine glycosylase II, MAG1 EC 3.2.2.22: rRNA 'N-glycosylase EC 3.2.2.23: DNA-formamidopyrimidine glycosylase EC 3.2.2.24: ADP-ribosyl-[dinitrogen reductase] hydrolase EC 3.2.2.25: N-methyl nucleosidase EC 3.2.2.26: futalosine hydrolase EC 3.2.2.27: uracil-DNA glycosylase EC 3.2.2.28: double-stranded uracil-DNA glycosylase EC 3.2.2.29: thymine-DNA glycosylase EC 3.2.2.30: aminodeoxyfutalosine nucleosidase * EC 3.2.2.31: adenine glycosylase * *No Wikipedia article === EC 3.2.3: Hydrolysing S-Glycosyl Compounds === Deleted sub-subclass == EC 3.3: Acting on Ether Bonds == === EC 3.3.1: Thioether and trialkylsulfonium hydrolases === EC 3.3.1.1: adenosylhomocysteinase EC 3.3.1.2: S-adenosyl-L-methionine hydrolase (L-homoserine-forming) EC 3.3.1.3: The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase === EC 3.3.2: Ether Hydrolases === EC 3.3.2.1: isochorismatase EC 3.3.2.2: alkenylglycerophosphocholine
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
hydrolase EC 3.3.2.3: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) EC 3.3.2.4: trans-epoxysuccinate hydrolase EC 3.3.2.5: Now included in EC 3.3.2.2, lysoplasmalogenase EC 3.3.2.6: leukotriene-A4 hydrolase EC 3.3.2.7: hepoxilin-epoxide hydrolase EC 3.3.2.8: limonene-1,2-epoxide hydrolase EC 3.3.2.9: microsomal epoxide hydrolase EC 3.3.2.10: soluble epoxide hydrolase EC 3.3.2.11: cholesterol-5,6-oxide hydrolase EC 3.3.2.12: oxepin-CoA hydrolase * EC 3.3.2.13: chorismatase * EC 3.3.2.14: 2,4-dinitroanisole O-demethylase * EC 3.3.2.15: trans-2,3-dihydro-3-hydroxyanthranilic acid synthase * *No Wikipedia article == EC 3.4: Acting on peptide bonds – Peptidase == === EC 3.4.1 α-amino acyl peptide hydrolases (discontinued) === EC 3.4.1.1: Now EC 3.4.11.1, leucyl aminopeptidase EC 3.4.1.2: Now EC 3.4.11.2, membrane alanyl aminopeptidase EC 3.4.1.3: Now EC 3.4.11.4, tripeptide aminopeptidase EC 3.4.1.4: Now EC 3.4.11.5, prolyl aminopeptidase === EC 3.4.2 Peptidyl amino acid hydrolases (discontinued) === EC 3.4.2.1: Now EC 3.4.17.1, carboxypeptidase A EC 3.4.2.2: Now EC 3.4.17.2, carboxypeptidase B EC 3.4.2.3: Now EC 3.4.17.4, Gly-Xaa carboxypeptidase === EC 3.4.3: Dipeptide hydrolases (deleted sub-subclass) === EC 3.4.3.1: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.3.2: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.3.3: Now EC 3.4.13.3, Xaa-His dipeptidase EC 3.4.3.4: Now EC 3.4.13.5, Xaa-methyl-His dipeptidase EC 3.4.3.5: Now EC 3.4.11.2, membrane alanyl aminopeptidase EC 3.4.3.6: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.3.7: Now EC 3.4.13.9, Xaa-Pro dipeptidase === EC 3.4.4 Peptidyl Peptide Hydrolases (discontinued) === EC 3.4.4.1: Now EC 3.4.23.1, pepsin A EC 3.4.4.2: Now EC 3.4.23.2, pepsin B EC 3.4.4.3: Now EC 3.4.23.4, chymosin EC 3.4.4.4: Now EC 3.4.21.4, trypsin EC 3.4.4.5: Now EC 3.4.21.1, chymotrypsin EC 3.4.4.6: Now EC 3.4.21.1, chymotrypsin EC 3.4.4.7: Now covered by EC 3.4.21.36, pancreatic elastase and EC 3.4.21.37, leukocyte elastase EC 3.4.4.8: Now EC 3.4.21.9, enteropeptidase EC 3.4.4.9: Now EC 3.4.14.1, dipeptidyl-peptidase I EC 3.4.4.10: Now EC 3.4.22.2, papain EC
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
3.4.4.11: Now EC 3.4.22.6, chymopapain EC 3.4.4.12: Now EC 3.4.22.3, ficain EC 3.4.4.13: Now EC 3.4.21.5, thrombin EC 3.4.4.14: Now EC 3.4.21.7, plasmin EC 3.4.4.15: Now EC 3.4.23.15, renin EC 3.4.4.16: Now covered by the microbial serine proteinases EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64 (endopeptidase K), EC 3.4.21.65 (thermomycolin), EC 3.4.21.66 (thermitase) and EC 3.4.21.67 (endopeptidase So) EC 3.4.4.17: Now covered by the microbial aspartic proteinases EC 3.4.23.20 (penicillopepsin), EC 3.4.23.21 (rhizopuspepsin), EC 3.4.23.22 (endothiapepsin), EC 3.4.23.23 (mucorpepsin), EC 3.4.23.24 (candidapepsin), EC 3.4.23.25 (saccharopepsin), EC 3.4.23.26 (rhodotorulapepsin), EC 3.4.21.103 (physarolisin), EC 3.4.23.28 (acrocylindropepsin), EC 3.4.23.29 (polyporopepsin) and EC 3.4.23.30 (pycnoporopepsin) EC 3.4.4.18: Now EC 3.4.22.10, streptopain EC 3.4.4.19: Now EC 3.4.24.3, microbial collagenase EC 3.4.4.20: Now EC 3.4.22.8, clostripain EC 3.4.4.21: Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) EC 3.4.4.22: Now EC 3.4.23.3, gastricsin EC 3.4.4.23: Now EC 3.4.23.5, cathepsin D EC 3.4.4.24: Now covered by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) EC 3.4.4.25: deleted === EC 3.4.11 Aminopeptidases === EC 3.4.11.1: leucyl aminopeptidase EC 3.4.11.2: membrane alanyl aminopeptidase EC 3.4.11.3: cystinyl aminopeptidase EC 3.4.11.4: tripeptide aminopeptidase EC 3.4.11.5: prolyl aminopeptidase EC 3.4.11.6: aminopeptidase B EC 3.4.11.7: glutamyl aminopeptidase EC 3.4.11.8: Now EC 3.4.19.3, pyroglutamyl-peptidase I EC 3.4.11.9: Xaa-Pro aminopeptidase EC 3.4.11.10: bacterial leucyl aminopeptidase EC 3.4.11.11: Deleted EC 3.4.11.12: Deleted EC 3.4.11.13: Clostridial aminopeptidase EC 3.4.11.14: cytosol alanyl aminopeptidase EC 3.4.11.15: aminopeptidase Y EC 3.4.11.16: Xaa-Trp aminopeptidase EC 3.4.11.17: tryptophanyl aminopeptidase EC 3.4.11.18: methionyl aminopeptidase EC 3.4.11.19: D-stereospecific aminopeptidase EC 3.4.11.20: aminopeptidase Ey EC 3.4.11.21: aspartyl aminopeptidase EC 3.4.11.22: aminopeptidase I EC 3.4.11.23: PepB aminopeptidase EC 3.4.11.24: aminopeptidase S EC 3.4.11.25: β-peptidyl aminopeptidase EC 3.4.11.26: intermediate cleaving peptidase 55 === EC 3.4.12 Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted sub-subclass) === EC 3.4.12.1: Now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
D) EC 3.4.12.2: Now EC 3.4.17.1, carboxypeptidase A EC 3.4.12.3: Now EC 3.4.17.2, carboxypeptidase B EC 3.4.12.4: Now EC 3.4.16.2, lysosomal Pro-Xaa carboxypeptidase EC 3.4.12.5: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.12.6: Now EC 3.4.17.8, muramoyl-pentapeptidase carboxypeptidase EC 3.4.12.7: Now EC 3.4.17.3, lysine carboxypeptidase EC 3.4.12.8: Now EC 3.4.17.4, Gly-Xaa carboxypeptidase EC 3.4.12.9: aspartate carboxypeptidase EC 3.4.12.10: Now EC 3.4.19.9, γ-glutamyl hydrolase EC 3.4.12.11: Now EC 3.4.17.6, alanine carboxypeptidase EC 3.4.12.12: Now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase D) EC 3.4.12.13: γ-glutamylglutamate carboxypeptidase === EC 3.4.13 Dipeptidases === EC 3.4.13.1: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.2: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.3: The activity is covered by EC .4.13.18, cytosol nonspecific dipeptidase and EC 3.4.13.20, β-Ala-His dipeptidase EC 3.4.13.4: Xaa-Arg dipeptidase EC 3.4.13.5: Xaa-methyl-His dipeptidase EC 3.4.13.6: Now EC 3.4.11.2, membrane alanyl aminopeptidase EC 3.4.13.7: Glu-Glu dipeptidase EC 3.4.13.8: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.9: Xaa-Pro dipeptidase EC 3.4.13.10: Now EC 3.4.19.5, β-aspartyl-peptidase EC 3.4.13.11: Now EC 3.4.13.19, membrane dipeptidase EC 3.4.13.12: Met-Xaa dipeptidase EC 3.4.13.13: Now EC 3.4.13.3, Xaa-His dipeptidase EC 3.4.13.14: Deleted EC 3.4.13.15: Now EC 3.4.13.18, cytosol nonspecific dipeptidase EC 3.4.13.16: Deleted EC 3.4.13.17: non-stereospecific dipeptidase EC 3.4.13.18: cytosol nonspecific dipeptidase EC 3.4.13.19: membrane dipeptidase EC 3.4.13.20: β-Ala-His dipeptidase EC 3.4.13.21: dipeptidase E EC 3.4.13.22: D-Ala-D-Ala dipeptidase EC 3.4.13.23: cysteinylglycine-S-conjugate dipeptidase * *No Wikipedia article === EC 3.4.14 Dipeptidyl peptidases and tripeptidyl peptidases === EC 3.4.14.1: dipeptidyl-peptidase I EC 3.4.14.2: dipeptidyl-peptidase II EC 3.4.14.3: Now EC 3.4.19.1, acylaminoacyl-peptidase EC 3.4.14.4: dipeptidyl-peptidase III EC 3.4.14.5: dipeptidyl-peptidase IV EC 3.4.14.6: dipeptidyl-dipeptidase EC 3.4.14.7: Deleted EC 3.4.14.8: Now EC 3.4.14.10, tripeptidyl-peptidase II EC 3.4.14.9: tripeptidyl-peptidase I EC 3.4.14.10: tripeptidyl-peptidase II EC 3.4.14.11: Xaa-Pro dipeptidyl-peptidase EC 3.4.14.12: Xaa-Xaa-Pro tripeptidyl-peptidase EC 3.4.14.13: γ-D-glutamyl-Llysine dipeptidyl-peptidase EC 3.4.14.14: [mycofactocin precursor peptide] peptidase * *No Wikipedia article
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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=== EC 3.4.15 Peptidyl dipeptidases === EC 3.4.15.1: peptidyl-dipeptidase A EC 3.4.15.2: Now EC 3.4.19.2, peptidyl-glycinamidase EC 3.4.15.3: Now EC 3.4.15.5, peptidyl-dipeptidase Dcp EC 3.4.15.4: Peptidyl-dipeptidase B EC 3.4.15.5: Peptidyl-dipeptidase Dcp EC 3.4.15.6: cyanophycinase === EC 3.4.16 Serine type carboxypeptidases === EC 3.4.16.1: Transferred entry: serine carboxypeptidase. Now EC 3.4.16.6, carboxypeptidase D EC 3.4.16.2: lysosomal Pro-Xaa carboxypeptidase EC 3.4.16.3: Now included with EC 3.4.16.5, carboxypeptidase C EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase EC 3.4.16.5: carboxypeptidase C EC 3.4.16.6: carboxypeptidase D === EC 3.4.17 Metallocarboxypeptidases === EC 3.4.17.1: carboxypeptidase A EC 3.4.17.2: carboxypeptidase B EC 3.4.17.3: lysine carboxypeptidase EC 3.4.17.4: Gly-Xaa carboxypeptidase EC 3.4.17.5: Deleted EC 3.4.17.6: alanine carboxypeptidase EC 3.4.17.7: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.17.8: muramoylpentapeptide carboxypeptidase EC 3.4.17.9: Now included with EC 3.4.17.4, Gly-Xaa carboxypeptidase EC 3.4.17.10: carboxypeptidase E EC 3.4.17.11: glutamate carboxypeptidase EC 3.4.17.12: carboxypeptidase M EC 3.4.17.13: Muramoyltetrapeptide carboxypeptidase EC 3.4.17.14: zinc D-Ala-D-Ala carboxypeptidase EC 3.4.17.15: carboxypeptidase A2 EC 3.4.17.16: membrane Pro-Xaa carboxypeptidase EC 3.4.17.17: tubulinyl-Tyr carboxypeptidase EC 3.4.17.18: carboxypeptidase T EC 3.4.17.19: Carboxypeptidase Taq EC 3.4.17.20: carboxypeptidase U EC 3.4.17.21: Glutamate carboxypeptidase II EC 3.4.17.22: metallocarboxypeptidase D EC 3.4.17.23: angiotensin-converting enzyme 2 EC 3.4.17.24: tubulin-glutamate carboxypeptidase * *No Wikipedia article === EC 3.4.18 Cysteine type carboxypeptidases === EC 3.4.18.1: cathepsin X === EC 3.4.19 Omega peptidases === EC 3.4.19.1: acylaminoacyl-peptidase EC 3.4.19.2: peptidyl-glycinamidase EC 3.4.19.3: pyroglutamyl-peptidase I EC 3.4.19.4: Deleted EC 3.4.19.5: β-aspartyl-peptidase EC 3.4.19.6: pyroglutamyl-peptidase II EC 3.4.19.7: N-formylmethionyl-peptidase EC 3.4.19.8: now EC 3.4.17.21, glutamate carboxypeptidase II EC 3.4.19.9: folate γ-glutamyl hydrolase EC 3.4.19.10: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase EC 3.4.19.11: γ-Dglutamyl-meso-diaminopimelate peptidase EC 3.4.19.12: ubiquitinyl hydrolase 1 EC 3.4.19.13: glutathione γ-glutamate hydrolase EC 3.4.19.14: leukotriene-C4 hydrolase EC 3.4.19.15: desampylase * EC 3.4.19.16: glucosinolate γ-glutamyl hydrolase * *No Wikipedia article === EC 3.4.21: Serine proteases === EC 3.4.21.1: chymotrypsin EC 3.4.21.2: chymotrypsin C EC
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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3.4.21.3: metridin EC 3.4.21.4: trypsin EC 3.4.21.5: thrombin EC 3.4.21.6: coagulation factor Xa EC 3.4.21.7: plasmin EC 3.4.21.8: Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) EC 3.4.21.9: enteropeptidase EC 3.4.21.10: acrosin EC 3.4.21.11: Now EC 3.4.21.37, leukocyte elastase EC 3.4.21.12: α-lytic endopeptidase EC 3.4.21.13: Now EC 3.4.16.6, carboxypeptidase D EC 3.4.21.14: now EC 3.4.21.67, endopeptidase So EC 3.4.21.15: Now EC 3.4.21.63, oryzin EC 3.4.21.16: Deleted EC 3.4.21.17: Deleted EC 3.4.21.18: Deleted EC 3.4.21.19: glutamyl endopeptidase EC 3.4.21.20: cathepsin G EC 3.4.21.21: coagulation factor VIIa EC 3.4.21.22: coagulation factor IXa EC 3.4.21.23: Deleted EC 3.4.21.24: Deleted EC 3.4.21.25: cucumisin EC 3.4.21.26: prolyl oligopeptidase EC 3.4.21.27: coagulation factor XIa EC 3.4.21.28: Now EC 3.4.21.74, venombin A EC 3.4.21.29: Now EC 3.4.21.74, venombin A EC 3.4.21.30: Now EC 3.4.21.74, venombin A EC 3.4.21.31: Now EC 3.4.21.73, u-plasminogen activator EC 3.4.21.32: brachyurin EC 3.4.21.33: Deleted EC 3.4.21.34: plasma kallikrein EC 3.4.21.35: tissue kallikrein EC 3.4.21.36: pancreatic elastase EC 3.4.21.37: leukocyte elastase EC 3.4.21.38: coagulation factor XIIa EC 3.4.21.39: chymase EC 3.4.21.40: Deleted EC 3.4.21.41: Complement subcomponent C1r EC 3.4.21.42: complement subcomponent C1s EC 3.4.21.43: classical-complement-pathway C3/C5 convertase EC 3.4.21.44: Now EC 3.4.21.43, classical-complement-pathway C3/C5 convertase EC 3.4.21.45: complement factor I EC 3.4.21.46: complement factor D EC 3.4.21.47: alternative-complement-pathway C3/C5 convertase EC 3.4.21.48: cerevisin EC 3.4.21.49: hypodermin C EC 3.4.21.50: lysyl endopeptidase EC 3.4.21.51: Deleted EC 3.4.21.52: Deleted EC 3.4.21.53: edopeptidase La EC 3.4.21.54: γ-renin EC 3.4.21.55: venombin AB EC 3.4.21.56: Now considered to be EC 3.4.21.25, cucumisin EC 3.4.21.57: leucyl endopeptidase EC 3.4.21.58: Deleted EC 3.4.21.59: tryptase EC 3.4.21.60: scutelarin EC 3.4.21.61: kexin EC 3.4.21.62: subtilisin EC 3.4.21.63: oryzin EC 3.4.21.64: endopeptidase K EC 3.4.21.65: thermomycolin EC 3.4.21.66: thermitase EC 3.4.21.67: endopeptidase So EC 3.4.21.68: t-plasminogen activator EC 3.4.21.69: protein C (activated) EC 3.4.21.70: pancreatic endopeptidase E EC 3.4.21.71: pancreatic elastase
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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II EC 3.4.21.72: IgA-specific serine endopeptidase EC 3.4.21.73: u-plasminogen activator EC 3.4.21.74: venombin A EC 3.4.21.75: furin EC 3.4.21.76: myeloblastin EC 3.4.21.77: semenogelase EC 3.4.21.78: granzyme A EC 3.4.21.79: granzyme B EC 3.4.21.80: streptogrisin A EC 3.4.21.81: streptogrisin B EC 3.4.21.82: glutamyl endopeptidase II EC 3.4.21.83: oligopeptidase B EC 3.4.21.84: limulus clotting factor C EC 3.4.21.85: limulus clotting factor B EC 3.4.21.86: limulus clotting enzyme EC 3.4.21.87: Now EC 3.4.23.49, omptin EC 3.4.21.88: repressor LexA EC 3.4.21.89: signal peptidase I EC 3.4.21.90: togavirin EC 3.4.21.91: flavivirin EC 3.4.21.92: endopeptidase Clp EC 3.4.21.93: proprotein convertase 1 EC 3.4.21.94: proprotein convertase 2 EC 3.4.21.95: snake venom factor V activator EC 3.4.21.96: lactocepin EC 3.4.21.97: assemblin EC 3.4.21.98: hepacivirin EC 3.4.21.99: spermosin EC 3.4.21.100: sedolisin EC 3.4.21.101: xanthomonalisin EC 3.4.21.102: C-terminal processing peptidase EC 3.4.21.103: physarolisin EC 3.4.21.104: mannan-binding lectin-associated serine protease-2 EC 3.4.21.105: rhomboid protease EC 3.4.21.106: hepsin EC 3.4.21.107: peptidase Do EC 3.4.21.108: HtrA2 peptidase EC 3.4.21.109: matriptase EC 3.4.21.110: C5a peptidase EC 3.4.21.111: aqualysin 1 EC 3.4.21.112: site-1 protease EC 3.4.21.113: pestivirus NS3 polyprotein peptidase EC 3.4.21.114: equine arterivirus serine peptidase EC 3.4.21.115: infectious pancreatic necrosis birnavirus Vp4 peptidase EC 3.4.21.116: SpoIVB peptidase EC 3.4.21.117: stratum corneum chymotryptic enzyme EC 3.4.21.118: kallikrein 8 EC 3.4.21.119: kallikrein 13 EC 3.4.21.120: oviductin EC 3.4.21.121: Lys-Lys/Arg-Xaa endopeptidase * *No Wikipedia article === EC 3.4.22 Cysteine proteases === EC 3.4.22.1: cathepsin B EC 3.4.22.2: papain EC 3.4.22.3: ficain EC 3.4.22.4: Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) EC 3.4.22.5: Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) EC 3.4.22.6: chymopapain EC 3.4.22.7: asclepain EC 3.4.22.8: clostripain EC 3.4.22.9: Now EC 3.4.21.48, cerevisin EC 3.4.22.10: streptopain EC 3.4.22.11: Now EC 3.4.24.56, insulysin EC 3.4.22.12: Now EC 3.4.19.9, γ-glutamyl hydrolase EC 3.4.22.13: Deleted EC 3.4.22.14: actinidain EC 3.4.22.15: cathepsin L EC
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{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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3.4.22.16: cathepsin H EC 3.4.22.17: Now EC 3.4.22.53, calpain-2 EC 3.4.22.18: Now EC 3.4.21.26, prolyl oligopeptidase EC 3.4.22.19: Now EC 3.4.24.15, thimet oligopeptidase EC 3.4.22.20: Deleted EC 3.4.22.21: Now EC 3.4.25.1, proteasome endopeptidase complex EC 3.4.22.22: Now EC 3.4.24.37, saccharolysin EC 3.4.22.23: Now EC 3.4.21.61, kexin EC 3.4.22.24: Cathepsin T EC 3.4.22.25: Glycyl endopeptidase EC 3.4.22.26: Cancer procoagulant EC 3.4.22.27: cathepsin S EC 3.4.22.28: picornain 3C EC 3.4.22.29: picornain 2A EC 3.4.22.30: Caricain EC 3.4.22.31: Ananain EC 3.4.22.32: Stem bromelain EC 3.4.22.33: Fruit bromelain EC 3.4.22.34: Legumain EC 3.4.22.35: Histolysain EC 3.4.22.36: caspase-1 EC 3.4.22.37: Gingipain R EC 3.4.22.38: Cathepsin K EC 3.4.22.39: adenain EC 3.4.22.40: bleomycin hydrolase EC 3.4.22.41: cathepsin F EC 3.4.22.42: cathepsin O EC 3.4.22.43: cathepsin V EC 3.4.22.44: nuclear-inclusion-a endopeptidase EC 3.4.22.45: helper-component proteinase EC 3.4.22.46: L-peptidase EC 3.4.22.47: gingipain K EC 3.4.22.48: staphopain EC 3.4.22.49: separase EC 3.4.22.50: V-cath endopeptidase EC 3.4.22.51: cruzipain EC 3.4.22.52: calpain-1 EC 3.4.22.53: calpain-2 EC 3.4.22.54: calpain-3 EC 3.4.22.55: caspase-2 EC 3.4.22.56: caspase-3 EC 3.4.22.57: caspase-4 EC 3.4.22.58: caspase-5 EC 3.4.22.59: caspase-6 EC 3.4.22.60: caspase-7 EC 3.4.22.61: caspase-8 EC 3.4.22.62: caspase-9 EC 3.4.22.63: caspase-10 EC 3.4.22.64: caspase-11 EC 3.4.22.65: peptidase 1 (mite) EC 3.4.22.66: calicivirin EC 3.4.22.67: zingipain EC 3.4.22.68: Ulp1 peptidase EC 3.4.22.69: SARS coronavirus main proteinase EC 3.4.22.70: sortase A EC 3.4.22.71: sortase B === EC 3.4.23 Aspartic endopeptidases === EC 3.4.23.1: pepsin A EC 3.4.23.2: pepsin B EC 3.4.23.3: gastricsin EC 3.4.23.4: chymosin EC 3.4.23.5: cathepsin D EC 3.4.23.6: Now EC 3.4.23.30, pycnoporopepsin EC 3.4.23.7: Now EC 3.4.23.20, penicillopepsin EC 3.4.23.8: Now EC 3.4.23.25, saccharopepsin EC 3.4.23.9: Now EC 3.4.23.21, rhizopuspepsin EC 3.4.23.10: Now EC 3.4.23.22, endothiapepsin EC 3.4.23.11: Deleted entry EC 3.4.23.12: nepenthesin EC 3.4.23.13: Deleted EC 3.4.23.14: Deleted EC 3.4.23.15: renin EC 3.4.23.16: HIV-1 retropepsin EC 3.4.23.17: pro-opiomelanocortin converting enzyme EC 3.4.23.18: aspergillopepsin I EC
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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3.4.23.19: aspergillopepsin II EC 3.4.23.20: penicillopepsin EC 3.4.23.21: rhizopuspepsin EC 3.4.23.22: endothiapepsin EC 3.4.23.23: mucorpepsin EC 3.4.23.24: candidapepsin EC 3.4.23.25: saccharopepsin EC 3.4.23.26: rhodotorulapepsin EC 3.4.23.27: Now EC 3.4.21.103, physarolisin EC 3.4.23.28: acrocylindropepsin EC 3.4.23.29: polyporopepsin EC 3.4.23.30: pycnoporopepsin EC 3.4.23.31: scytalidopepsin A EC 3.4.23.32: scytalidopepsin B EC 3.4.23.33: Now EC 3.4.21.101, xanthomonalisin EC 3.4.23.34: cathepsin E EC 3.4.23.35: barrierpepsin EC 3.4.23.36: signal peptidase II EC 3.4.23.37: Now EC 3.4.21.100, pseudomonalisin EC 3.4.23.38: plasmepsin I EC 3.4.23.39: plasmepsin II EC 3.4.23.40: phytepsin EC 3.4.23.41: yapsin 1 EC 3.4.23.42: thermopsin EC 3.4.23.43: prepilin peptidase EC 3.4.23.44: nodavirus endopeptidase EC 3.4.23.45: memapsin 1 EC 3.4.23.46: memapsin 2 EC 3.4.23.47: HIV-2 retropepsin EC 3.4.23.48: plasminogen activator Pla EC 3.4.23.49: omptin EC 3.4.23.50: human endogenous retrovirus K endopeptidase EC 3.4.23.51: HycI peptidase EC 3.4.23.52: preflagellin peptidase === EC 3.4.24: Metallopeptidases === EC 3.4.24.1: atrolysin A EC 3.4.24.2: Deleted entry: Sepia proteinase EC 3.4.24.3: microbial collagenase EC 3.4.24.4: now EC 3.4.24.40 serralysin EC 3.4.24.5: Deleted entry: lens neutral proteinase. Now included with EC 3.4.22.53 (calpain-2) and EC 3.4.25.1 (proteasome endopeptidase complex) EC 3.4.24.6: leucolysin EC 3.4.24.7: interstitial collagenase EC 3.4.24.8: Transferred entry: Achromobacter iophagus collagenase. Now EC 3.4.24.3, microbial collagenase EC 3.4.24.9: Deleted entry: Trichophyton schoenleinii collagenase EC 3.4.24.10: Deleted entry: Trichophyton mentagrophytes keratinase EC 3.4.24.11: neprilysin EC 3.4.24.12: envelysin EC 3.4.24.13: IgA-specific metalloendopeptidase EC 3.4.24.14: procollagen N-endopeptidase EC 3.4.24.15: thimet oligopeptidase EC 3.4.24.16: neurolysin EC 3.4.24.17: stromelysin 1 EC 3.4.24.18: meprin A EC 3.4.24.19: procollagen C-endopeptidase EC 3.4.24.20: peptidyl-Lys metalloendopeptidase EC 3.4.24.21: astacin EC 3.4.24.22: stromelysin 2 EC 3.4.24.23: matrilysin EC 3.4.24.24: gelatinase a EC 3.4.24.25: vibriolysin EC 3.4.24.26: pseudolysin EC 3.4.24.27: thermolysin EC 3.4.24.28: bacillolysin EC 3.4.24.29: aureolysin EC 3.4.24.30: coccolysin EC 3.4.24.31: mycolysin EC 3.4.24.32: β-lytic metalloendopeptidase EC 3.4.24.33: peptidyl-Asp metalloendopeptidase EC 3.4.24.34: neutrophil collagenase EC 3.4.24.35: gelatinase B EC 3.4.24.36: leishmanolysin
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
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EC 3.4.24.37: saccharolysin EC 3.4.24.38: gametolysin EC 3.4.24.39: deuterolysin EC 3.4.24.40: serralysin EC 3.4.24.41: atrolysin B EC 3.4.24.42: atrolysin C EC 3.4.24.43: atroxase EC 3.4.24.44: atrolysin E EC 3.4.24.45: atrolysin F EC 3.4.24.46: adamalysin EC 3.4.24.47: horrilysin EC 3.4.24.48: ruberlysin EC 3.4.24.49: bothropasin EC 3.4.24.50: bothrolysin EC 3.4.24.51: ophiolysin EC 3.4.24.52: trimerelysin I EC 3.4.24.53: trimerelysin II EC 3.4.24.54: mucrolysin EC 3.4.24.55: pitrilysin EC 3.4.24.56: insulysin EC 3.4.24.57: O-sialoglycoprotein endopeptidase EC 3.4.24.58: russellysin EC 3.4.24.59: mitochondrial intermediate peptidase EC 3.4.24.60: dactylysin EC 3.4.24.61: nardilysin EC 3.4.24.62: magnolysin EC 3.4.24.63: meprin B EC 3.4.24.64: mitochondrial processing peptidase EC 3.4.24.65: macrophage elastase EC 3.4.24.66: choriolysin L EC 3.4.24.67: choriolysin H EC 3.4.24.68: tentoxilysin EC 3.4.24.69: bontoxilysin EC 3.4.24.70: oligopeptidase A EC 3.4.24.71: endothelin-converting enzyme 1 EC 3.4.24.72: fibrolase EC 3.4.24.73: jararhagin EC 3.4.24.74: fragilysin EC 3.4.24.75: lysostaphin EC 3.4.24.76: flavastacin EC 3.4.24.77: snapalysin EC 3.4.24.78: gpr endopeptidase EC 3.4.24.79: pappalysin-1 EC 3.4.24.80: membrane-type matrix metalloproteinase-1 EC 3.4.24.81: ADAM10 endopeptidase EC 3.4.24.82: ADAMTS-4 endopeptidase EC 3.4.24.83: anthrax lethal factor endopeptidase EC 3.4.24.84: Ste24 endopeptidase EC 3.4.24.85: S2P endopeptidase EC 3.4.24.86: ADAM 17 endopeptidase EC 3.4.24.87: ADAMTS13 endopeptidase === EC 3.4.25 Threonine endopeptidases === EC 3.4.25.1: proteasome endopeptidase complex EC 3.4.25.2: HslU—HslV peptidase EC 3.4.99.7: Deleted entry: euphorbain EC 3.4.99.8: Deleted entry: Gliocladium proteinase EC 3.4.99.9: Deleted entry: hurain. Now considered to be EC 3.4.21.25, cucumisin EC 3.4.99.10: Transferred entry: insulinase. Now EC 3.4.24.56, insulysin EC 3.4.99.11: Deleted entry: Streptomyces alkalophilic keratinase EC 3.4.99.12: Deleted entry: Trichophyton mentagrophytes keratinase EC 3.4.99.13: Transferred entry: β-lytic proteinase (Mycobacterium sorangium). Now EC 3.4.24.32 EC 3.4.24.32, β-lytic metalloendopeptidase EC 3.4.99.14: Deleted entry: mexicanain EC 3.4.99.15: Deleted entry: Paecilomyces proteinase EC 3.4.99.16: Deleted entry: Penicillium notatum extracellular proteinase EC 3.4.99.17: Deleted entry: peptidoglycan endopeptidase EC 3.4.99.18: Deleted entry: pinguinain EC 3.4.99.19: Transferred entry: renin. Now EC 3.4.23.15, renin EC
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
3.4.99.20: Deleted entry: scopulariopsis proteinase EC 3.4.99.21: Deleted entry: solanain. Now considered EC 3.4.21.25, cucumisin EC 3.4.99.22: Transferred entry: staphylokinase. EC 3.4.24.29, aureolysin EC 3.4.99.23: Deleted entry: tabernamontanain. Now considered EC 3.4.21.25, cucumisin EC 3.4.99.24: Deleted entry: Tenebrio α-proteinase EC 3.4.99.25: Transferred entry: trametes acid proteinase. EC 3.4.23.21, rhizopuspepsin EC 3.4.99.26: Transferred entry: urokinase. Now EC 3.4.21.68, t-plasminogen activator EC 3.4.99.27: Deleted entry: Echis carinatus prothrombin-activating proteinase EC 3.4.99.28: Transferred entry: Oxyuranus scutellatus prothrombin-activating proteinase. EC 3.4.21.60 EC 3.4.21.60, scutelarin EC 3.4.99.29: Deleted entry: Myxobacter AL-1 proteinase I EC 3.4.99.30: Transferred entry: Myxobacter AL-1 proteinase II. EC 3.4.24.20, peptidyl-Lys metalloendopeptidase EC 3.4.99.31: Transferred entry: tissue endopeptidase degrading collagenase synthetic substrate. EC 3.4.24.15, thimet oligopeptidase EC 3.4.99.32: Transferred entry: Armillaria mellea neutral proteinase. Now EC 3.4.24.20, peptidyl-Lys metalloendopeptidase EC 3.4.99.33: Deleted entry: cathepsin R EC 3.4.99.34: Deleted entry: mytilidase EC 3.4.99.35: Transferred entry: premurein-leader peptidase. Now EC 3.4.23.36, signal peptidase II EC 3.4.99.36: Transferred entry: leader peptidase. Now EC 3.4.21.89, signal peptidase I EC 3.4.99.37: Deleted entry: RecA peptidase EC 3.4.99.38: Transferred entry: pro-opiomelanotropin-converting proteinase. Now EC 3.4.23.17, pro-opiomelanocortin converting enzyme EC 3.4.99.39: Deleted entry: pseudomurein endopeptidase EC 3.4.99.40: Deleted entry: pro-gonadoliberin proteinase EC 3.4.99.41: Transferred entry: mitochondrial processing peptidase. Now EC 3.4.24.64, mitochondrial processing peptidase EC 3.4.99.42: Deleted entry: leucyllysine endopeptidase EC 3.4.99.43: Transferred entry: thermopsin. Npw EC 3.4.23.42, thermopsin EC 3.4.99.44: Transferred entry: pitrilysin. Now EC 3.4.24.55, pitrilysin EC 3.4.99.45: Transferred entry: insulinase. Now EC 3.4.24.56, insulysin EC 3.4.99.46: Transferred entry: multicatalytic endopeptidase complex. Now EC 3.4.25.1, proteasome endopeptidase complex == EC 3.5: Acting on carbon-nitrogen bonds, other than peptide bonds == === 3.5.1: In linear amides === EC 3.5.1.1: asparaginase EC 3.5.1.2: glutaminase EC 3.5.1.3: ω-amidase EC 3.5.1.4: amidase EC 3.5.1.5: urease EC 3.5.1.6: β-ureidopropionase EC 3.5.1.7: ureidosuccinase EC 3.5.1.8: formylaspartate deformylase EC 3.5.1.9: arylformamidase EC 3.5.1.10: formyltetrahydrofolate
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
deformylase EC 3.5.1.11: penicillin amidase EC 3.5.1.12: biotinidase EC 3.5.1.13: aryl-acylamidase EC 3.5.1.14: N-acyl-aliphatic-L-amino acid amidohydrolase EC 3.5.1.15: aspartoacylase EC 3.5.1.16: acetylornithine deacetylase EC 3.5.1.17: acyl-lysine deacylase EC 3.5.1.18: succinyl-diaminopimelate desuccinylase EC 3.5.1.19: nicotinamidase EC 3.5.1.20: citrullinase EC 3.5.1.21: N-acetyl-β-alanine deacetylas EC 3.5.1.22: pantothenase EC 3.5.1.23: ceramidase EC 3.5.1.24: choloylglycine hydrolase EC 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase EC 3.5.1.26: N4-(β-N-acetylglucosaminyl)-L-asparaginase EC 3.5.1.27: The activity is covered by EC 3.5.1.88, peptide deformylase EC 3.5.1.28: N-acetylmuramoyl-L-alanine amidase EC 3.5.1.29: 2-(acetamidomethylene)succinate hydrolase EC 3.5.1.30: 5-aminopentanamidase EC 3.5.1.31: formylmethionine deformylase EC 3.5.1.32: hippurate hydrolase EC 3.5.1.33: N-acetylglucosamine deacetylase EC 3.5.1.34: Identical with EC 3.4.13.5, Xaa-methyl-His dipeptidase EC 3.5.1.35: D-glutaminase EC 3.5.1.36: N-methyl-2-oxoglutaramate hydrolase EC 3.5.1.37: Delete, identical with EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase EC 3.5.1.38: glutamin-(asparagin-)ase EC 3.5.1.39: alkylamidase EC 3.5.1.40: acylagmatine amidase EC 3.5.1.41: chitin deacetylase EC 3.5.1.42: nicotinamide-nucleotide amidase EC 3.5.1.43: peptidyl-glutaminase EC 3.5.1.44: protein-glutamine glutaminase EC 3.5.1.45: Now listed only as EC 6.3.4.6 urea carboxylase EC 3.5.1.46: 6-aminohexanoate-dimer hydrolase EC 3.5.1.47: N-acetyldiaminopimelate deacetylase EC 3.5.1.48: acetylspermidine deacetylase EC 3.5.1.49: formamidase EC 3.5.1.50: pentanamidase EC 3.5.1.51: 4-acetamidobutyryl-CoA deacetylase EC 3.5.1.52: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase EC 3.5.1.53: N-carbamoylputrescine amidase EC 3.5.1.54: allophanate hydrolase EC 3.5.1.55: long-chain-fatty-acyl-glutamate deacylase EC 3.5.1.56: N,N-dimethylformamidase EC 3.5.1.57: tryptophanamidase EC 3.5.1.58: N-benzyloxycarbonylglycine hydrolase EC 3.5.1.59: N-carbamoylsarcosine amidase EC 3.5.1.60: N-(long-chain-acyl)ethanolamine deacylase EC 3.5.1.61: mimosinase EC 3.5.1.62: acetylputrescine deacetylase EC 3.5.1.63: 4-acetamidobutyrate deacetylase EC 3.5.1.64: Nα-benzyloxycarbonylleucine hydrolase EC 3.5.1.65: theanine hydrolase EC 3.5.1.66: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase EC 3.5.1.67: 4-methyleneglutaminase EC 3.5.1.68: N-formylglutamate deformylase EC 3.5.1.69: glycosphingolipid deacylase EC 3.5.1.70: aculeacin-A deacylase EC 3.5.1.71: N-feruloylglycine deacylase EC 3.5.1.72: D-benzoylarginine-4-nitroanilide amidase EC 3.5.1.73: carnitinamidase EC 3.5.1.74: chenodeoxycholoyltaurine hydrolase EC 3.5.1.75: urethanase EC 3.5.1.76: arylalkyl acylamidase EC 3.5.1.77: N-carbamoyl-D-amino-acid hydrolase EC 3.5.1.78: glutathionylspermidine amidase EC 3.5.1.79: phthalyl amidase EC 3.5.1.80: Identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase EC 3.5.1.81: N-acyl-D-amino-acid deacylase EC 3.5.1.82: N-acyl-D-glutamate deacylase EC 3.5.1.83: N-acyl-D-aspartate deacylase EC 3.5.1.84:
|
{
"page_id": 5506847,
"source": null,
"title": "List of EC numbers (EC 3)"
}
|
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