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https://en.wikipedia.org/wiki/GPR110 | Probable G-protein coupled receptor 110 is a protein that in humans is encoded by the GPR110 gene. This gene encodes a member of the adhesion-GPCR receptor family. Family members are characterized by an extended extracellular region with a variable number of N-terminal protein modules coupled to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR133 | Probable G-protein coupled receptor 133 is a protein that in humans is encoded by the GPR133 gene.
This gene encodes a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR150 | Probable G-protein coupled receptor 150 is a protein that in humans is encoded by the GPR150 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/P2RY8 | P2Y purinoceptor 8 is a protein that in humans is encoded by the P2RY8 gene.
Function
The protein encoded by this gene belongs to the family of G-protein coupled receptors, that are preferentially activated by adenosine and uridine nucleotides. This gene is moderately expressed in undifferentiated HL60 cells, and is located on both chromosomes X and Y.
Clinical relevance
Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.
See also
P2Y receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/VN1R2 | Vomeronasal type-1 receptor 2 is a protein that in humans is encoded by the VN1R2 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/VN1R3 | Vomeronasal type-1 receptor 3 is a protein that is encoded by the VN1R3 gene in humans.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/VN1R4 | Vomeronasal type-1 receptor 4 is a protein that in humans is encoded by the VN1R4 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/VN1R5 | Vomeronasal type-1 receptor 5 is a protein that in humans is encoded by the VN1R5 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/TAAR6 | Trace amine associated receptor 6, also known as TAAR6, is a protein which in humans is encoded by the TAAR6 gene.
Function
TAAR6 belongs to the trace amine-associated receptor family. Trace amines are endogenous amine compounds that are chemically similar to classic biogenic amines like dopamine, norepinephrine, serotonin, and histamine. Trace amines were thought to be 'false transmitters' that displace classic biogenic amines from their storage and act on transporters in a fashion similar to the amphetamines, but the identification of brain receptors specific to trace amines indicates that they also have effects of their own. RNA expression analysis shows hTAAR6 is expressed in the hippocampus, where murine TAAR receptors have been shown to be involved with neurogenesis.
Computational modeling suggests TAAR6 can bind to the foul smelling compounds produced by rotting flesh, putrescine and cadaverine.
TAAR6 mutant mice have differences in behavior compared with wild-type mice. Also, they have elevated brain serotonin levels in several brain regions and enhanced hypothermic response to 5-HT1A receptor agonist 8-OH-DPAT.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Hydroxycarboxylic%20acid%20receptor%202 | Hydroxycarboxylic acid receptor 2 (HCA2), also known as GPR109A and niacin receptor 1 (NIACR1), is a protein which in humans is encoded (its formation is directed) by the HCAR2 gene and in rodents by the Hcar2 gene. The human HCAR2 gene is located on the long (i.e., "q") arm of chromosome 12 at position 24.31 (notated as 12q24.31). Like the two other hydroxycarboxylic acid receptors, HCA1 and HCA3, HCA2 is a G protein-coupled receptor (GPCR) located on the surface membrane of cells. HCA2 binds and thereby is activated by D-β-hydroxybutyric acid (hereafter termed β-hydroxybutyric acid), butyric acid, and niacin (also known as nicotinic acid). β-Hydroxybutyric and butyric acids are regarded as the endogenous agents that activate HCA2. Under normal conditions, niacin's blood levels are too low to do so: it is given as a drug in high doses in order to reach levels that activate HCA2.
β-Hydroxybutyric acid, butyric acid, and niacin have actions that are independent of HCA2. For example: 1) β-hydroxybutyric acid activates free fatty acid receptor 3 and inhibits some histone deacetylases that regulate the expression of various genes, increase mitochondrial adenosine triphosphate production, and promote antioxidant defenses; 2) butyric acid activates free fatty acid receptor 2 and like β-hydroxybutyric acid activates free fatty acid receptor 3 and inhibits some histone deacetylases; and 3) niacin is an NAD precursor (see nicotinamide adenine dinucleotide) which when converted to NAD |
https://en.wikipedia.org/wiki/Relaxin/insulin-like%20family%20peptide%20receptor%204 | Relaxin/insulin-like family peptide receptor 4, also known as RXFP4, is a human G-protein coupled receptor.
Function
GPR100 is a member of the rhodopsin family of G protein-coupled receptors (GPRs) (Fredriksson et al., 2003).[supplied by OMIM]
See also
Relaxin receptor
References
External links
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Frank%E2%80%93Read%20source | In materials science, a Frank–Read source is a mechanism explaining the generation of multiple dislocations in specific well-spaced slip planes in crystals when they are deformed. When a crystal is deformed, in order for slip to occur, dislocations must be generated in the material. This implies that, during deformation, dislocations must be primarily generated in these planes. Cold working of metal increases the number of dislocations by the Frank–Read mechanism. Higher dislocation density increases yield strength and causes work hardening of metals.
The mechanism of dislocation generation was proposed by and named after British physicist Charles Frank and Thornton Read.
History
Charles Frank detailed the history of the discovery from his perspective in Proceedings of the Royal Society in 1980.
In 1950 Charles Frank, who was then a research fellow in the physics department at the University of Bristol, visited the United States to participate in a conference on crystal plasticity in Pittsburgh. Frank arrived in the United States well in advance of the conference to spend time at a naval laboratory and to give a lecture at Cornell University. When, during his travels in Pennsylvania, Frank visited Pittsburgh, he received a letter from fellow scientist Jock Eshelby suggesting that he read a recent paper by Gunther Leibfried. Frank was supposed to board a train to Cornell to give his lecture at Cornell, but before departing for Cornell he went to the library at Carnegie |
https://en.wikipedia.org/wiki/GPR149 | Probable G-protein coupled receptor 149 is a protein that in humans is encoded by the GPR149 gene.
References
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR144 | Probable G-protein coupled receptor 144 is a protein that in humans is encoded by the GPR144 gene. This gene encodes a member of the adhesion-GPCR family of receptors. Family members are characterised by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR141 | Probable G-protein coupled receptor 141 is a protein that in humans is encoded by the GPR141 gene.
GPR141 is a member of the rhodopsin family of G protein-coupled receptors (GPRs).
References
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR153 | Probable G-protein coupled receptor 153 is a protein that in humans is encoded by the GPR153 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR152 | Probable G-protein coupled receptor 152 is a protein that in humans is encoded by the GPR152 gene.
Model organisms
Model organisms have been used in the study of GPR152 function. A conditional knockout mouse line called Gpr152tm1b(EUCOMM)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed: - In-depth immunological phenotyping
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/DaT%20scan | DaT Scan (DaT scan or Dopamine Transporter Scan) commonly refers to a diagnostic method to investigate if there is a loss of dopaminergic neurons in striatum. The term may also refer to a brand name of Ioflupane (123I) which is used for the study. The scan principle is based on use of the radiopharmaceutical Ioflupane (123I) which binds to dopamine transporters (DaT). The signal from them is then detected by the use of single-photon emission computed tomography (SPECT) which uses special gamma-cameras to create a pictographic representation of the distribution of dopamine transporters in the brain.
DaTSCAN is indicated in cases of tremor when its origin is uncertain. Although this method can distinguish essential tremor from Parkinson's syndrome, it is unable to distinguish between Parkinson's disease, multiple system atrophy or progressive supranuclear palsy.
There is evidence that DaTSCAN is accurate in diagnosing early Parkinson's.
Procedure
At the beginning a patient should take two iodine tablets and wait for one hour. These pills are important because they prevent the accumulation of radioactive substances in the thyroid gland. After one hour, the patient gets an injection to the shoulder, which contains the radiopharmaceutical, and then waits for 4 hours. The concentration of the substance increases, and then it is scanned by a gamma-camera, which is located around the patient's head. The whole examination lasts about 30–45 minutes, and it is non-invasive.
If a pa |
https://en.wikipedia.org/wiki/Sean%20Scannell | Sean Scannell (born 17 September 1990) is a professional footballer who plays as a winger for Isthmian League Premier Division club Hornchurch.
Scannell began his career with Crystal Palace where he scored 12 goals in 130 League appearances between 2007 and 2012. He then signed for Huddersfield Town where he spent the next six seasons. He has since played for Burton Albion, Bradford City, Blackpool and Grimsby Town. He has represented the Republic of Ireland at U17, U18, U19, U21 and B level.
Club career
Crystal Palace
Scannell joined Palace at 14 and notched 23 goals for the academy during the 2006–07 season, graduating to the reserves before breaking into the first team in the 2007–08 season. Scannell made his debut for Crystal Palace in a 2–1 win at London rivals QPR in December 2007 as a substitute. In his home debut against Sheffield Wednesday on 15 December, he again came on as a substitute in the second half and scored a 90th-minute winner, his first senior goal in a 2–1 victory for Crystal Palace. He finished that campaign having featured in 25 games, earning him a call up to the Republic of Ireland Under-17's squad and was named Palace's Young Player of the Year in 2008.
Following this, Scannell was offered a two and a half year professional contract with Palace. Scannell signed the contract at the beginning of the new year, and celebrated by scoring Palace's second goal in a 3–0 victory against Wolverhampton Wanderers the following weekend.
At the end of the 20 |
https://en.wikipedia.org/wiki/FLAME%20clustering | Fuzzy clustering by Local Approximation of MEmberships (FLAME) is a data clustering algorithm that defines clusters in the dense parts of a dataset and performs cluster assignment solely based on the neighborhood relationships among objects. The key feature of this algorithm is that the neighborhood relationships among neighboring objects in the feature space are used to constrain the memberships of neighboring objects in the fuzzy membership space.
Description of the FLAME algorithm
The FLAME algorithm is mainly divided into three steps:
Extraction of the structure information from the dataset:
Construct a neighborhood graph to connect each object to its K-Nearest Neighbors (KNN);
Estimate a density for each object based on its proximities to its KNN;
Objects are classified into 3 types:
Cluster Supporting Object (CSO): object with density higher than all its neighbors;
Cluster Outliers: object with density lower than all its neighbors, and lower than a predefined threshold;
the rest.
Local/Neighborhood approximation of fuzzy memberships:
Initialization of fuzzy membership:
Each CSO is assigned with fixed and full membership to itself to represent one cluster;
All outliers are assigned with fixed and full membership to the outlier group;
The rest are assigned with equal memberships to all clusters and the outlier group;
Then the fuzzy memberships of all type 3 objects are updated by a converging iterative procedure called Local/Neighborhood Approximation of F |
https://en.wikipedia.org/wiki/NU-Tech | NU-Tech is a digital signal processing (DSP) platform to validate and real-time debug complex algorithms, simply relying on a common PC. It is based on a typical plug-in architecture and thanks to a free software development kit (SDK), the developer can write his own plug-in (aka NUTSs = NU-Tech Satellites) in C++.
NUTSs are not compelled to provide a GUI. To ease the developer in quickly creating new NUTSs without having to deal with GUI programming, NU-Tech provides a window called "RealTime Watch" to be associated to each NUTS (a tab on the NU-Tech bottom Multitab pane).
The developer chooses, by code, whether to "expose" some NUTSs' internal variables on this window, in order to control his plug-in.
NU-Tech can connect to the external world by means of interchangeable drivers. For audio real-time applications ASIO 2.1 has been adopted in order to guarantee minimum and repeatable latencies, fully exploiting compatible sound cards hardware resources.
NU-Tech is freeware for non-commercial use.
Available features
Audio streaming
Video streaming and synchronization mechanism
Virtual Studio Technology support
ASIO 2.1 support
DirectX support
Performance_analysis information
Free SDK
References
Papers about NU-Tech applications
See also
Digital audio editors
Acoustics software
Windows-only freeware |
https://en.wikipedia.org/wiki/Anthropogenic%20biome | Anthropogenic biomes, also known as anthromes, human biomes or intensive land-use biome, describe the terrestrial biosphere (biomes) in its contemporary, human-altered form using global ecosystem units defined by global patterns of sustained direct human interaction with ecosystems. Anthromes are generally composed of heterogeneous mosaics of different land uses and land covers, including significant areas of fallow or regenerating habitats.
Origin and evolution of the concept
Anthromes were first named and mapped by Erle Ellis and Navin Ramankutty in their 2008 paper, "Putting People in the Map: Anthropogenic Biomes of the World". Anthrome maps now appear in numerous textbooks. and in the National Geographic World Atlas. The most recent version of anthrome maps were published in 2021.
In a recent global ecosystem classification, anthropogenic biomes have been incorporated into several distinct functional biomes in the terrestrial and freshwater realms, and additional units have been described for the freshwater, marine, subterranean and transitional realms to create a more comprehensive description of all ecosystems created and maintained by human activities. The intensive land-use biome comprises five distinct terrestrial ecosystem functional groups: pastures, crops, plantations, urban and semi-natural ecosystem functional group. The artificial wetlands biome in the freshwater realm includes large reservoirs and other constructed wetlands, rice paddies, aquafarms and ne |
https://en.wikipedia.org/wiki/Nucleotide%20diphosphatase | In enzymology, a nucleotide diphosphatase () is an enzyme that catalyzes the chemical reaction
a dinucleotide + H2O 2 mononucleotides
Thus, the two substrates of this enzyme are dinucleotide and H2O, whereas its product is mononucleotide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dinucleotide nucleotidohydrolase. Other names in common use include nucleotide pyrophosphatase, and nucleotide-sugar pyrophosphatase. This enzyme participates in 5 metabolic pathways: purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis.
Structural studies
, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Oligopeptide-transporting%20ATPase | In enzymology, an oligopeptide-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + oligopeptide(out) ADP + phosphate + oligopeptide(in)
The 3 substrates of this enzyme are ATP, H2O, and oligopeptide, whereas its 3 products are ADP, phosphate, and oligopeptide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (oligopeptide-importing). This enzyme is also called oligopeptide permease.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oligosaccharide-diphosphodolichol%20diphosphatase | In enzymology, an oligosaccharide-diphosphodolichol diphosphatase () is an enzyme that catalyzes the chemical reaction
oligosaccharide-diphosphodolichol + H2O oligosaccharide phosphate + dolichyl phosphate
Thus, the two substrates of this enzyme are oligosaccharide-diphosphodolichol and H2O, whereas its two products are oligosaccharide phosphate and dolichyl phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is oligosaccharide-diphosphodolichol phosphodolichohydrolase. This enzyme is also called oligosaccharide-diphosphodolichol pyrophosphatase.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oligosaccharide-transporting%20ATPase | In enzymology, an oligosaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + oligosaccharideout ADP + phosphate + oligosaccharidein
The 3 substrates of this enzyme are ATP, H2O, and oligosaccharide, whereas its 3 products are ADP, phosphate, and oligosaccharide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (disaccharide-importing).
References
EC 3.6.3
Enzymes of unknown structure
Transport proteins
Transmembrane proteins
Transmembrane transporters |
https://en.wikipedia.org/wiki/Peptide-transporting%20ATPase | In enzymology, a peptide-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + peptidein ADP + phosphate + peptideout
The 3 substrates of this enzyme are ATP, H2O, and peptide, whereas its 3 products are ADP, phosphate, and peptide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (peptide-exporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peroxisome-assembly%20ATPase | In enzymology, a peroxisome-assembly ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate. Its function is to transport components of the peroxisome in and out of the organelle.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (peroxisome-assembling). This enzyme is also called peroxisome assembly factor-2.
References
EC 3.6.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphate-transporting%20ATPase | In enzymology, a phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + phosphate(out) ADP + phosphate + phosphate(in)
The 3 substrates of this enzyme are ATP, H2O, and phosphate, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phosphate-importing). This enzyme is also called ABC phosphate transporter. This enzyme participates in abc transporters - general.
References
EC 7.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoadenylylsulfatase | In enzymology, a phosphoadenylylsulfatase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + H2O adenosine 3',5'-bisphosphate + sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and H2O, whereas its two products are adenosine 3',5'-bisphosphate and sulfate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in sulfonyl-containing anhydrides. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate sulfohydrolase. Other names in common use include 3-phosphoadenylyl sulfatase, 3-phosphoadenosine 5-phosphosulfate sulfatase, PAPS sulfatase, and 3'-phosphoadenylylsulfate sulfohydrolase. This enzyme participates in sulfur metabolism. It employs one cofactor, manganese.
References
EC 3.6.2
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phospholipid-translocating%20ATPase | In enzymology, a phospholipid-translocating ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + phospholipid in ADP + phosphate + phospholipid out
The 3 substrates of this enzyme are ATP, H2O, and phospholipid, whereas its 3 products are ADP, phosphate, and phospholipid.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phospholipid-flipping). Other names in common use include Mg2+-ATPase, flippase, and aminophospholipid-transporting ATPase.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphonate-transporting%20ATPase | In enzymology, a phosphonate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + phosphonateout ADP + phosphate + phosphonatein
The 3 substrates of this enzyme are ATP, H2O, and phosphonate, whereas its 3 products are ADP, phosphate, and phosphonate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (phosphonate-transporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoribosyl-ATP%20diphosphatase | In enzymology, a phosphoribosyl-ATP diphosphatase () is an enzyme that catalyzes the chemical reaction
1-(5-phosphoribosyl)-ATP + H2O 1-(5-phosphoribosyl)-AMP + diphosphate
Thus, the two substrates of this enzyme are 1-(5-phosphoribosyl)-ATP and H2O, whereas its two products are 1-(5-phosphoribosyl)-AMP and diphosphate.
This enzyme participates in histidine metabolism. It employs one cofactor, H+.
Nomenclature
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is 1-(5-phosphoribosyl)-ATP diphosphohydrolase. Other names in common use include phosphoribosyl-ATP pyrophosphatase, and phosphoribosyladenosine triphosphate pyrophosphatase.
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Polar-amino-acid-transporting%20ATPase | In enzymology, a polar-amino-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + polar amino acidout ADP + phosphate + polar amino acidin
The 3 substrates of this enzyme are ATP, H2O, and polar amino acid, whereas its 3 products are ADP, phosphate, and polar amino acid.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polar-amino-acid-importing). This enzyme is also called histidine permease. This enzyme participates in abc transporters - general.
References
EC 7.4.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Polyamine-transporting%20ATPase | In enzymology, a polyamine-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + polyamineout ADP + phosphate + polyaminein
The 3 substrates of this enzyme are ATP, H2O, and polyamine, whereas its 3 products are ADP, phosphate, and polyamine.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (polyamine-importing). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Proteasome%20ATPase | In enzymology, a proteasome ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (polypeptide-degrading).
References
EC 3.6.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-secreting%20ATPase | In enzymology, a protein-secreting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (protein-secreting).
See also
SecY protein
Translocon
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quaternary-amine-transporting%20ATPase | In enzymology, a quaternary-amine-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + quaternary amineout ADP + phosphate + quaternary aminein
The 3 substrates of this enzyme are ATP, H2O, and quaternary amine, whereas its 3 products are ADP, phosphate, and quaternary amine.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (quaternary-amine-importing). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sulfate-transporting%20ATPase | In enzymology, a sulfate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + sulfateout ADP + phosphate + sulfatein
The 3 substrates of this enzyme are ATP, H2O, and sulfate, whereas its 3 products are ADP, phosphate, and sulfate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (sulfate-importing). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Taurine-transporting%20ATPase | In enzymology, a taurine-transporting ATPase () is an enzyme that catalyzes the chemical reaction.
ATP + H2O + taurineout ADP + phosphate + taurinein
The 3 substrates of this enzyme are ATP, H2O, and taurine, whereas its 3 products are ADP, phosphate, and taurine.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (taurine-importing).
References
Further reading
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Teichoic-acid-transporting%20ATPase | In enzymology, a teichoic-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + teichoic acidin ADP + phosphate + teichoic acidout
The 3 substrates of this enzyme are ATP, H2O, and teichoic acid, whereas its 3 products are ADP, phosphate, and teichoic acid.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (teichoic-acid-exporting). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiamine-triphosphatase | Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction
thiamine triphosphate + H2O thiamine diphosphate + phosphate
This enzyme belongs to the family of acid anhydride hydrolases, specifically those acting on phosphorus-containing anhydrides. Its systematic name is thiamine triphosphate phosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
See also
Thiamine-diphosphate kinase
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Northern%20hardwood%20forest | The northern hardwood forest is a general type of North American forest ecosystem found over much of southeastern and south-central Canada, Ontario, and Quebec, extending south into the United States in northern New England, New York, and Pennsylvania, and west along the Great Lakes to Minnesota and western Ontario. Some ecologists consider it a transitional forest because it contains species common to both the oak-hickory forest community to the south and the Boreal forest community to the north. The trees and shrub species of the Northern Hardwood Forest are known for their brilliant fall colors, making the regions that contain this forest type popular fall foliage tourist destinations.
Sugar maple, yellow birch, American beech, and white ash are the common key indicator tree and shrub species in the Northern Hardwood Forest. Other species include eastern hemlock and eastern white pine. Herb and heath species include wintergreen, wild sarsaparilla, and wood sorrel. Birds and animals common to the Northern Hardwood Forest include the black-capped chickadee, white-throated sparrow, cedar waxwing, porcupine, snowshoe hare, white-tailed deer, and American red squirrel.
Most of the Northern Hardwood Forest is not virgin forest, it is regrowth following centuries of commercial timber harvesting and the clearing of land for agricultural purposes. This is particularly true of New England, New York, and Eastern Canada, where the land was cleared to make room for farms in the 17th |
https://en.wikipedia.org/wiki/Thymidine-triphosphatase | In enzymology, a thymidine-triphosphatase () is an enzyme that catalyzes the chemical reaction
dTTP + H2O dTDP + phosphate
Thus, the two substrates of this enzyme are dTTP and H2O, whereas its two products are dTDP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dTTP nucleotidohydrolase. Other names in common use include thymidine triphosphate nucleotidohydrolase, dTTPase, and deoxythymidine-5'-triphosphatase. This enzyme participates in pyrimidine metabolism.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Trimetaphosphatase | In enzymology, a trimetaphosphatase () is an enzyme that catalyzes the chemical reaction
trimetaphosphate + H2O triphosphate
Thus, the two substrates of this enzyme are trimetaphosphate and H2O, whereas its product is triphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is trimetaphosphate hydrolase. This enzyme is also called inorganic trimetaphosphatase. This enzyme participates in pyrimidine metabolism.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Triphosphatase | In enzymology, a triphosphatase () is an enzyme that catalyzes the chemical reaction
triphosphate + H2O diphosphate + phosphate
Thus, the two substrates of this enzyme are triphosphate and H2O, whereas its two products are diphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is triphosphate phosphohydrolase. This enzyme is also called inorganic triphosphatase.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-sugar%20diphosphatase | In enzymology, an UDP-sugar diphosphatase () is an enzyme that catalyzes the chemical reaction
UDP-sugar + H2O UMP + alpha-D-aldose 1-phosphate
Thus, the two substrates of this enzyme are UDP-sugar and H2O, whereas its two products are UMP and alpha-D-aldose 1-phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is UDP-sugar sugarphosphohydrolase. Other names in common use include nucleosidediphosphate-sugar pyrophosphatase, nucleosidediphosphate-sugar diphosphatase, UDP-sugar hydrolase, and UDP-sugar pyrophosphatase.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Undecaprenyl-diphosphatase | In enzymology, an undecaprenyl-diphosphatase () is an enzyme that catalyzes the chemical reaction
undecaprenyl diphosphate + H2O undecaprenyl phosphate + phosphate
Thus, the two substrates of this enzyme are undecaprenyl diphosphate and H2O, whereas its two products are undecaprenyl phosphate and phosphate. The enzymatic activity is enhanced by divalent cations, particularly Ca2+.
In many bacteria, this enzyme is a membrane protein that participates in peptidoglycan biosynthesis. The enzyme has been implicated in conferring resistance to the antibiotic bacitracin.
Nomenclature
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is undecaprenyl-diphosphate phosphohydrolase. Other names in common use include Undecaprenyl-pyrophosphate phosphatase (Uppp), UPP phosphatase, BacA, C55-isoprenyl diphosphatase, C55-isoprenyl pyrophosphatase, and isoprenyl pyrophosphatase.
Note: The enzyme Uppp/BacA (EC 3.6.1.27) has occasionally been incorrectly termed an "undecaprenol kinase". However, that name should be reserved for a distinct enzyme (EC 2.7.1.66), which catalyses the addition of a phosphate group from ATP to undecaprenol (C55-isoprenyl alcohol).
Structure
X-ray crystal structures of the membrane-form of the enzyme from E. coli are available (PDB IDs: 5OON, 6CB2).
References
Further reading
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vesicle-fusing%20ATPase | In enzymology, a vesicle-fusing ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (vesicle-fusing).
References
EC 3.6.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Vitamin%20B12-transporting%20ATPase | {{DISPLAYTITLE:Vitamin B12-transporting ATPase}}
In enzymology, a vitamin B12-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + vitamin B12out ADP + phosphate + vitamin B12in
The 3 substrates of this enzyme are ATP, H2O, and vitamin B12, whereas its 3 products are ADP, phosphate, and vitamin B12.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (vitamin B12-importing). This enzyme participates in abc transporters - general.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Xenobiotic-transporting%20ATPase | In enzymology, a xenobiotic-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + xenobioticin ADP + phosphate + xenobioticout
The 3 substrates of this enzyme are ATP, H2O, and xenobiotic, whereas its 3 products are ADP, phosphate, and xenobiotic.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (xenobiotic-exporting). Other names in common use include multidrug-resistance protein, MDR protein, P-glycoprotein, pleiotropic-drug-resistance protein, PDR protein, steroid-transporting ATPase, and ATP phosphohydrolase (steroid-exporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Zn2%2B-exporting%20ATPase | In enzymology, a Zn2+-exporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Zn2+in ADP + phosphate + Zn2+out
The 3 substrates of this enzyme are ATP, H2O, and Zn2+, whereas its 3 products are ADP, phosphate, and Zn2+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Zn2+-exporting). Other names in common use include Zn(II)-translocating P-type ATPase, P1B-type ATPase, and AtHMA4 (the A. thaliana protein).
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and . Moreover, nanobodies have recently been raised against a zinc-transporting ATPase (ZntA) which are able to bind and inhibit the ATPase activity, showing potential for further structural studies.
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Trk%20receptor | Trk receptors are a family of tyrosine kinases that regulates synaptic strength and plasticity in the mammalian nervous system. Trk receptors affect neuronal survival and differentiation through several signaling cascades. However, the activation of these receptors also has significant effects on functional properties of neurons.
The common ligands of trk receptors are neurotrophins, a family of growth factors critical to the functioning of the nervous system. The binding of these molecules is highly specific. Each type of neurotrophin has different binding affinity toward its corresponding Trk receptor. The activation of Trk receptors by neurotrophin binding may lead to activation of signal cascades resulting in promoting survival and other functional regulation of cells.
Origin of the name trk
The abbreviation trk (often pronounced 'track') stands for tropomyosin receptor kinase or tyrosine receptor kinase (and not "tyrosine kinase receptor" nor "tropomyosin-related kinase", as has been commonly mistaken).
The family of Trk receptors is named for the oncogene trk, whose identification led to the discovery of its first member, TrkA. Trk, initially identified in a colon carcinoma, is frequently (25%) activated in thyroid papillary carcinomas. The oncogene was generated by a mutation in chromosome 1 that resulted in the fusion of the first seven exons of tropomyosin to the transmembrane and cytoplasmic domains of the then-unknown TrkA receptor. Normal Trk receptors do not |
https://en.wikipedia.org/wiki/11-cis-retinyl-palmitate%20hydrolase | The enzyme 11-cis-retinyl-palmitate hydrolase (EC 3.1.1.63) catalyzes the reaction
11-cis-retinyl palmitate + H2O 11-cis-retinol + palmitate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 11-cis-retinyl-palmitate acylhydrolase. Other names in common use include 11-cis-retinol palmitate esterase, and RPH. This enzyme participates in retinol metabolism. This enzyme has at least one effector, Bile salt.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1%2C4-lactonase | The enzyme 1,4-lactonase (EC 3.1.1.25) catalyzes the generic reaction
a 1,4-lactone + H2O a 4-hydroxyacid
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 1,4-lactone hydroxyacylhydrolase. It is also called γ-lactonase. It participates in galactose metabolism and ascorbate and aldarate metabolism. It employs one cofactor, Ca2+.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes , , and .
Applications
In a study by Chen et al. a 1,4-lactonase was expressed in E. coli and used as a highly efficient biocatalyst for asymmetric synthesis of chiral compounds.
References
EC 3.1.1
Calcium enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/1-alkyl-2-acetylglycerophosphocholine%20esterase | The enzyme 1-alkyl-2-acetylglycerophosphocholine esterase (EC 3.1.1.47) catalyzes the reaction
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O 1-alkyl-sn-glycero-3-phosphocholine + acetate
The former is also known as platelet-activating factor. There are multiple enzymes with this function:
Lipoprotein-associated phospholipase A2
Platelet-activating factor acetylhydrolase 2, cytoplasmic
Platelet-activating factor acetylhydrolase 1b: regulatory subunit 1, catalytic subunit 2, catalytic subunit 3
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetohydrolase. Other names in common use include 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase, and alkylacetyl-GPC:acetylhydrolase. This enzyme participates in ether lipid metabolism.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2%27%2C3%27-cyclic-nucleotide%202%27-phosphodiesterase | The enzyme 2′,3′-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) catalyzes the reaction
nucleoside 2′,3′-cyclic phosphate + H2O nucleoside 3′-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is nucleoside-2′,3′-cyclic-phosphate 3'-nucleotidohydrolase. Other names in common use include ribonucleoside 2′,3′-cyclic phosphate diesterase, 2′,3′-cyclic AMP phosphodiesterase, 2′,3′-cyclic nucleotidase, cyclic 2′,3′-nucleotide 2′-phosphodiesterase, cyclic 2′,3′-nucleotide phosphodiesterase, 2′,3′-cyclic nucleoside monophosphate phosphodiesterase, 2′,3′-cyclic AMP 2′-phosphohydrolase, cyclic phosphodiesterase:3′-nucleotidase, 2′,3′-cyclic nucleotide phosphohydrolase, 2′:3′-cyclic phosphodiesterase, and 2′:3′-cyclic nucleotide phosphodiesterase:3'-nucleotidase. This enzyme participates in purine metabolism and pyrimidine metabolism.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-Carboxy-D-arabinitol-1-phosphatase | The enzyme 2-carboxy-D-arabinitol-1-phosphatase (CA1Pase; EC 3.1.3.63) catalyzes the reaction
2-carboxy-D-arabinitol 1-phosphate + H2O 2-carboxy-D-arabinitol + phosphate
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name is 2-carboxy-D-arabinitol-1-phosphate 1-phosphohydrolase.
In biology
The best-studied 2-Carboxy-D-arabinitol-1-phosphate phosphatase is the enzyme that inactivates the RuBisCO inhibitor 2-carboxy-D-arabinitol-1-phosphate (CA1P).
When light levels are high, the inactivation occurs after CA1P has been released from RuBisCO by RuBisCO activase. As CA1P is present in many but not all plants, CA1P-mediated regulation of RuBisCO is not universal for all photosynthetic life. Amino acid sequences of the CA1Pase enzymes from wheat, French bean, tobacco, and Arabidopsis thaliana reveal that the enzymes contain 2 different domains, indicating that it is a multifunctional enzyme.
CA1Pase enzyme activity varies between different species due to their regulation by different redox-active compounds, such as glutathione. However, it is yet to be determined whether this process occurs in vivo. Wheat CA1Pase heterologously expressed in E. coli is also able to dephosphorylate the RuBisCO inhibitor D-glycero-2,3-diulose-1,5-bisphosphate.
References
Further reading
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-deoxyglucose-6-phosphatase | The enzyme 2-deoxyglucose-6-phosphatase (EC 3.1.3.68) catalyzes the reaction
2-deoxy-D-glucose 6-phosphate + H2O 2-deoxy-D-glucose + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 2-deoxy-D-glucose-6-phosphate phosphohydrolase. This enzyme is also called 2-deoxyglucose-6-phosphate phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-phosphosulfolactate%20phosphatase | The enzyme 2-phosphosulfolactate phosphatase (EC 3.1.3.71) catalyzes the reaction
(2R)-2-phospho-3-sulfolactate + H2O (2R)-3-sulfolactate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name (R)-2-phospho-3-sulfolactate phosphohydrolase. Other names in common use include (2R)-phosphosulfolactate phosphohydrolase, and ComB phosphatase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-pyrone-4%2C6-dicarboxylate%20lactonase | The enzyme 2-pyrone-4,6-dicarboxylate lactonase (EC 3.1.1.57, LigI) catalyzes the reversible hydrolytic reaction
2-oxo-2H-pyran-4,6-dicarboxylate + H2O = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
This enzyme belongs to the Amidohydrolase superfamily of enzymes and is a member of Cluster of Orthologous Groups (COG) 3618. The systematic name of this enzyme is 2-oxo-2H-pyran-4,6-dicarboxylate lactonohydrolase. This enzyme is found to play an important role in the metabolism of lignin-derived aromatic compounds in both the syringate degradation pathway and the protocatechuate 4,5-cleavage pathway.
LigI from Sphingomonas is of particular interest as it has been shown to be the first member of the amidohydrolase superfamily to not require a divalent metal cation for catalytic activity.
Mechanism
The mechanism of catalysis of LigI has been determined by crystallography and NMR analysis. More specifically, the hydrolytic water molecule is activated by the transfer of a proton to Asp-248 whereas the carbonyl group of the 2-pyrone-4,6-dicarboxylate (PDC) lactone substrate is activated by hydrogen bonding interactions with His-180, His-31, and His-33.
References
Further reading
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/3%27%282%27%29%2C5%27-bisphosphate%20nucleotidase | The enzyme 3′(2′),5′-bisphosphate nucleotidase (EC 3.1.3.7) catalyzes the reaction
adenosine 3′,5′-bisphosphate + H2O AMP + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosine-3′(2′),5′-bisphosphate 3′(2′)-phosphohydrolase. Other names in common use include phosphoadenylate 3′-nucleotidase, 3′-phosphoadenylylsulfate 3′-phosphatase, and 3′(2′),5′-bisphosphonucleoside 3′(2′)-phosphohydrolase. This enzyme participates in sulfur metabolism.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/3%27%2C5%27-cyclic-GMP%20phosphodiesterase | The enzyme 3′,5′-cyclic-GMP phosphodiesterase (EC 3.1.4.35) catalyzes the reaction
guanosine 3′,5′-cyclic phosphate + H2O guanosine 5′-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 3′,5′-cyclic-GMP 5'-nucleotidohydrolase. Other names in common use include guanosine cyclic 3',5'-phosphate phosphodiesterase, cyclic GMP phosphodiesterase, cyclic 3′,5′-GMP phosphodiesterase, cyclic guanosine 3′,5′-monophosphate phosphodiesterase, cyclic guanosine 3′,5′-phosphate phosphodiesterase, cGMP phosphodiesterase, cGMP-PDE, and cyclic guanosine 3′,5′-phosphate phosphodiesterase.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 3.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate-8-phosphatase | The enzyme 3-deoxy-manno-octulosonate-8-phosphatase (EC 3.1.3.45) catalyzes the reaction
3-deoxy-D-manno-octulosonate 8-phosphate + H2O 3-deoxy-D-manno-octulosonate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3-deoxy-D-manno-octulosonate-8-phosphate 8-phosphohydrolase. This enzyme participates in lipopolysaccharide biosynthesis.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-hydroxyisobutyryl-CoA%20hydrolase | The enzyme 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) catalyzes the reaction
3-hydroxy-2-methylpropanoyl-CoA + H2O CoA + 3-hydroxy-2-methylpropanoate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is 3-hydroxy-2-methylpropanoyl-CoA hydrolase. Other names in common use include 3-hydroxy-isobutyryl CoA hydrolase, and HIB CoA deacylase. This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, β-alanine metabolism, and propanoate metabolism. 3-hydroxyisobutyryl-CoA hydrolase is encoded by HIBCH gene.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%27-nucleotidase | The enzyme 3′-nucleotidase (EC 3.1.3.6) the reaction
a 3′-ribonucleotide + H2O a ribonucleoside + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3′-ribonucleotide phosphohydrolase. Other names in common use include 3′-mononucleotidase, 3′-phosphatase, and 3′-ribonucleotidase. This enzyme participates in purine and pyrimidine metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-oxoadipate%20enol-lactonase | The enzyme 3-oxoadipate enol-lactonase (EC 3.1.1.24) catalyzes the reaction
3-oxoadipate enol-lactone + H2O 3-oxoadipate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase. Other names in common use include carboxymethylbutenolide lactonase, β-ketoadipic enol-lactone hydrolase, 3-ketoadipate enol-lactonase, 3-oxoadipic enol-lactone hydrolase, and β-ketoadipate enol-lactone hydrolase. This enzyme participates in benzoate degradation via hydroxylation.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-phosphoglycerate%20phosphatase | The enzyme 3-phosphoglycerate phosphatase (EC 3.1.3.38) catalyzes the reaction
D-glycerate 3-phosphate + H2O D-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-glycerate-3-phosphate phosphohydrolase. Other names in common use include D-3-Phosphoglycerate phosphatase, and 3-PGA phosphatase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-phytase | The enzyme 3-phytase (EC 3.1.3.8) catalyzes the reaction
myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
myo-Inositol hexakisphosphate is also known as phytic acid.
These enzymes belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name myo-inositol-hexakisphosphate 3-phosphohydrolase. Other names in common use include 1-phytase, phytate 1-phosphatase, phytate 3-phosphatase, and phytate 6-phosphatase.
Enzymes of this type participate in inositol phosphate metabolism.
Structural studies
As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , and .
See also
4-phytase (6-phytase)
5-phytase
Protein tyrosine phosphatase
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA%20thioesterase | The enzyme 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) catalyzes the reaction
4-hydroxybenzoyl-CoA + H2O 4-hydroxybenzoate + CoA
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is 4-hydroxybenzoyl-CoA hydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .
References
EC 3.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-methyloxaloacetate%20esterase | The enzyme 4-methyloxaloacetate esterase (EC 3.1.1.44) catalyzes the reaction
oxaloacetate 4-methyl ester + H2O oxaloacetate + methanol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is oxaloacetate-4-methyl-ester oxaloacetohydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/VHDL-AMS | VHDL-AMS is a derivative of the hardware description language VHDL (IEEE standard 1076-1993). It includes analog and mixed-signal extensions (AMS) in order to define the behavior of analog and mixed-signal systems (IEEE 1076.1-1999).
The VHDL-AMS standard was created with the intent of enabling designers of analog and mixed signal systems and integrated circuits to create and use modules that encapsulate high-level behavioral descriptions as well as structural descriptions of systems and components.
VHDL-AMS is an industry standard modeling language for mixed signal circuits. It provides both continuous-time and event-driven modeling semantics, and so is suitable for analog, digital, and mixed analog/digital circuits. It is particularly well suited for verification of very complex analog, mixed-signal and radio frequency integrated circuits.
Code example
In VHDL-AMS, a design consists at a minimum of an entity which describes the interface and an architecture which contains the actual implementation. In addition, most designs import library modules. Some designs also contain multiple architectures and configurations.
A simple ideal diode in VHDL-AMS would look something like this:
library IEEE;
use IEEE.math_real.all;
use IEEE.electrical_systems.all;
-- this is the entity
entity DIODE is
generic (iss : current := 1.0e-14);
port (terminal anode, cathode : electrical);
end entity DIODE;
architecture IDEAL of DIODE is
quantity v across i through anode |
https://en.wikipedia.org/wiki/Pinning%20points | In a crystalline material, a dislocation is capable of traveling throughout the lattice when relatively small stresses are applied. This movement of dislocations results in the material plastically deforming. Pinning points in the material act to halt a dislocation's movement, requiring a greater amount of force to be applied to overcome the barrier. This results in an overall strengthening of materials.
Types of pinning points
Point defects
Point defects (as well as stationary dislocations, jogs, and kinks) present in a material create stress fields within a material that disallow traveling dislocations to come into direct contact. Much like two particles of the same electric charge feel a repulsion to one another when brought together, the dislocation is pushed away from the already present stress field.
Alloying elements
The introduction of atom1 into a crystal of atom2 creates a pinning point for multiple reasons. An alloying atom is by nature a point defect, thus it must create a stress field when placed into a foreign crystallographic position, which could block the passage of a dislocation. However, it is possible that the alloying material is approximately the same size as the atom that is replaced, and thus its presence would not stress the lattice (as occurs in cobalt alloyed nickel). The different atom would, though, have a different elastic modulus, which would create a different terrain for the moving dislocation. A higher modulus would look like an energy ba |
https://en.wikipedia.org/wiki/4-nitrophenylphosphatase | The enzyme 4-nitrophenylphosphatase (EC 3.1.3.41) catalyzes the reaction
4-nitrophenyl phosphate + H2O 4-nitrophenol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 4-nitrophenylphosphate phosphohydrolase. Other names in common use include nitrophenyl phosphatase, p-nitrophenylphosphatase, ''para-nitrophenyl phosphatase, K-pNPPase, NPPase, PNPPase, Ecto-p-nitrophenyl phosphatase, and p''-nitrophenylphosphate phosphohydrolase. This enzyme participates in γ-hexachlorocyclohexane degradation.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-phytase | The enzyme 4-phytase () catalyzes the following reaction:
myo-inositol hexakisphosphate + H2O 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
myo-Inositol hexakisphosphate is also known as phytic acid.
These enzymes belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is myo-inositol-hexakisphosphate 4-phosphohydrolase. Other names in common use include 6-phytase (name based on 1L-numbering system and not 1D-numbering) and phytate 6-phosphatase.
Enzymes of this type participate in inositol phosphate metabolism.
See also
3-phytase (1-phytase)
5-phytase
Protein tyrosine phosphatase
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/4-pyridoxolactonase | The enzyme 4-pyridoxolactonase (EC 3.1.1.27) catalyzes the reaction
4-pyridoxolactone + H2O 4-pyridoxate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-pyridoxolactone lactonohydrolase. It participates in vitamin B6 metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-%283%2C4-diacetoxybut-1-ynyl%29-2%2C2%27-bithiophene%20deacetylase | The enzyme 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene deacetylase (EC 3.1.1.66) catalyzes the reaction
5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene + H2O 5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2′-bithiophene + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene acetylhydrolase. Other names in common use include diacetoxybutynylbithiophene acetate esterase, and 3,4-diacetoxybutinylbithiophene:4-acetate esterase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/5-phytase | The enzyme 5-phytase (EC 3.1.3.72) catalyzes the reaction
myo-inositol hexakisphosphate + H2O = 1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate
myo-Inositol hexakisphosphate is also known as phytic acid.
These enzymes belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is myo-inositol-hexakisphosphate 5-phosphohydrolase.
Prevalence
Of the hundreds of phytase enzymes that have been characterized in the literature, only two have been characterized as 5-phytases. A histidine acid phosphatases purified from lily pollen and a protein tyrosine phosphatase-like phytase from Selenomonas ruminantium subsp. lactilytica were both found to have specificity for the 5-phosphate position of myo-inositol hexakisphosphate.
Structural studies
As of late 2007, only the phytase purified from lily pollen had its structure solved, with PDB accession codes , , , , , and .
See also
3-phytase (1-phytase)
4-phytase (6-phytase)
Protein tyrosine phosphatase
References
EC 3.1.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/6-acetylglucose%20deacetylase | The enzyme 6-acetylglucose deacetylase (EC 3.1.1.33) catalyzes the reaction
6-acetyl-D-glucose + H2O D-glucose + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 6-acetyl-D-glucose acetylhydrolase. This enzyme is also called 6-O-acetylglucose deacetylase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoacetyl-CoA%20hydrolase | The enzyme acetoacetyl-CoA hydrolase (EC 3.1.2.11) catalyzes the reaction
acetoacetyl-CoA + H2O CoA + acetoacetate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is acetoacetyl-CoA hydrolase. Other names in common use include acetoacetyl coenzyme A hydrolase, acetoacetyl CoA deacylase, and acetoacetyl coenzyme A deacylase. This enzyme participates in butanoate metabolism.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetoxybutynylbithiophene%20deacetylase | The enzyme acetoxybutynylbithiophene deacetylase (EC 3.1.1.54) catalyzes the reaction
5-(4-acetoxybut-1-ynyl)-2,2′-bithiophene + H2O 5-(4-hydroxybut-1-ynyl)-2,2′-bithiophene + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 5-(4-acetoxybut-1-ynyl)-2,2′-bithiophene O-acetylhydrolase. Other names in common use include acetoxybutynylbithiophene esterase, and 5-(4-acetoxy-1-butynyl)-2,2′-bithiophene:acetate esterase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylalkylglycerol%20acetylhydrolase | The enzyme acetylalkylglycerol acetylhydrolase (EC 3.1.1.71) catalyzes the reaction
2-acetyl-1-alkyl-sn-glycerol + H2O 1-alkyl-sn-glycerol + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 2-acetyl-1-alkyl-sn-glycerol acetylhydrolase. This enzyme is also called alkylacetylglycerol acetylhydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28acetyl-CoA%20carboxylase%29-phosphatase | The enzyme [acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) catalyzes the reaction
[acetyl-CoA carboxylase] phosphate + HO [acetyl-CoA carboxylase] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetyl-CoA%20hydrolase | The enzyme acetyl-CoA hydrolase (EC 3.1.2.1) catalyzes the reaction
acetyl-CoA + H2O CoA + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is CoA thiol esterase. This enzyme participates in pyruvate metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
See also
Acetyl-CoA synthetase and ACSS2, enzymes that perform the reverse reaction using ATP
References
EC 3.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetylesterase | In biochemistry, an acetylesterase () is a class of enzyme which catalyzes the hydrolysis of acetic esters into an alcohol and acetic acid:
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds (esterases). The systematic name of this enzyme class is acetic-ester acetylhydrolase. Other names in common use include C-esterase (in animal tissues), acetic ester hydrolase, chloroesterase, p-nitrophenyl acetate esterase, and citrus acetylesterase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetylsalicylate%20deacetylase | The enzyme acetylsalicylate deacetylase (EC 3.1.1.55) catalyzes the reaction
acetylsalicylate + H2O salicylate + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is acetylsalicylate O-acetylhydrolase. Other names in common use include aspirin esterase, acetylsalicylic acid esterase, and aspirin hydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylxylan%20esterase | The enzyme acetylxylan esterase (EC 3.1.1.72) catalyzes the deacetylation of xylans and xylo-oligosaccharides.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic nameis acetylxylan esterase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.1.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Actinomycin%20lactonase | The enzyme actinomycin lactonase (EC 3.1.1.39) catalyzes the reaction
actinomycin + H2O actinomycinic monolactone
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is actinomycin lactonohydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acylcarnitine%20hydrolase | The enzyme acylcarnitine hydrolase (EC 3.1.1.28) catalyzes the reaction
O-acylcarnitine + H2O a fatty acid + L-carnitine
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is O-acylcarnitine acylhydrolase. Other names in common use include high activity acylcarnitine hydrolase, HACH, carnitine ester hydrolase, palmitoylcarnitine hydrolase, palmitoyl-L-carnitine hydrolase, long-chain acyl-L-carnitine hydrolase, and palmitoyl carnitine hydrolase.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28acyl-carrier-protein%29%20phosphodiesterase | The enzyme [acyl-carrier-protein] phosphodiesterase (EC 3.1.4.14) catalyzes the reaction
holo-[acyl-carrier-protein] + HO 4′-phosphopantetheine + apo-[acyl-carrier-protein]
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. Other names in common use include ACP hydrolyase, ACP phosphodiesterase, AcpH, and [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. This enzyme participates in pantothenate and CoA biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acyl-CoA%20hydrolase | The enzyme acyl-CoA hydrolase (EC 3.1.2.20) catalyzes the reaction
acyl-CoA + H2O CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is acyl-CoA hydrolase. Other names in common use include acyl coenzyme A thioesterase, acyl-CoA thioesterase, acyl coenzyme A hydrolase, thioesterase B, thioesterase II, and acyl-CoA thioesterase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.1.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acyloxyacyl%20hydrolase | The enzyme acyloxyacyl hydrolase (EC 3.1.1.77, AOAH) was discovered because it catalyzes the reaction
3-(acyloxy)acyl group of bacterial toxin + H2O = 3-hydroxyacyl group of bacterial toxin + a fatty acid
The enzyme removes from lipid A the secondary acyl chains that are needed for lipopolysaccharides to be recognized by the MD-2--TLR4 receptor on animal cells. This reaction inactivates the lipopolysaccharide (endotoxin); the tetraacyl lipid A product can inhibit LPS signaling.
Acyloxyacyl hydrolase is produced by monocyte-macrophages, neutrophils, dendritic cells, NK cells, ILC1 cells, and renal cortical tubule cells. It is a protein of about 60 kDa that has two disulfide-linked subunits. The smaller subunit, of about 14 kDa (including glycosylation), is a member of the SAPLIP (saposin-like protein) family along with amoebapore, granulysin, acid sphingomyelinase, surfactant protein B, and the 4 sphingolipid activator proteins (saposins). The larger subunit, of 50 kDa, contains the active site serine and the other elements of the His-Asp-Ser triad; AOAH is a GDSL lipase that has activity toward certain glycerolipids in addition to its presumed major in vivo substrate, LPS.
Also see "AOAH".
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Adenylyl-%28glutamate%E2%80%94ammonia%20ligase%29%20hydrolase | In enzymology, an adenylyl-[glutamate---ammonia ligase] hydrolase () is an enzyme that catalyzes the chemical reaction
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
Thus, the two substrates of this enzyme are [[adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]]] and H2O, whereas its two products are adenylate and L-glutamate:ammonia ligase (ADP-forming).
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] adenylylhydrolase. Other names in common use include adenylyl-[glutamine-synthetase]hydrolase, and adenylyl(glutamine synthetase) hydrolase.
References
EC 3.1.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ADP-dependent%20medium-chain-acyl-CoA%20hydrolase | The enzyme ADP-dependent medium-chain-acyl-CoA hydrolase (EC 3.1.2.19) catalyzes the reaction
acyl-CoA + H2O CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is ADP-dependent-medium-chain-acyl-CoA hydrolase. Other names in common use include medium-chain acyl coenzyme A hydrolase, medium-chain acyl-CoA hydrolase, medium-chain acyl-thioester hydrolase, medium-chain hydrolase, and myristoyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound, NADH is known to inhibit this enzyme.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ADP-dependent%20short-chain-acyl-CoA%20hydrolase | The enzyme ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18) catalyzes the reaction
acyl-CoA + H2O CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is ADP-dependent-short-chain-acyl-CoA hydrolase. Other names in common use include short-chain acyl coenzyme A hydrolase, propionyl coenzyme A hydrolase, propionyl-CoA hydrolase, propionyl-CoA thioesterase, short-chain acyl-CoA hydrolase, and short-chain acyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound, NADH is known to inhibit this enzyme.
References
EC 3.1.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ADP-phosphoglycerate%20phosphatase | The enzyme ADP-phosphoglycerate phosphatase (EC 3.1.3.28) catalyzes the reaction
3-(ADP)-2-phosphoglycerate + H2O 3-(ADP)-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3-(ADP)-2-phosphoglycerate phosphohydrolase. This enzyme is also called adenosine diphosphate phosphoglycerate phosphatase.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylacetylglycerophosphatase | The enzyme alkylacetylglycerophosphatase (EC 3.1.3.59) catalyzes the reaction
1-alkyl-2-acetyl-sn-glycero-3-phosphate + H2O 1-alkyl-2-acetyl-sn-glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-alkyl-2-acetyl-sn-glycero-3-phosphate phosphohydrolase. Other names in common use include 1-alkyl-2-lyso-sn-glycero-3-P:acetyl-CoA acetyltransferase, and alkylacetylglycerophosphate phosphatase. This enzyme participates in ether lipid metabolism.
References
EC 3.1.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylglycerophosphoethanolamine%20phosphodiesterase | The enzyme alkylglycerophosphoethanolamine phosphodiesterase (EC 3.1.4.39) catalyzes the reaction
1-alkyl-sn-glycero-3-phosphoethanolamine + H2O 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase. This enzyme is also called lysophospholipase D. This enzyme participates in ether lipid metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.1.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/All-trans-retinyl-palmitate%20hydrolase | The enzyme retinoid isomerohydrolase (EC 3.1.1.64, all-trans-retinyl-palmitate hydrolase) catalyzes the reaction
an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is ''all-trans-retinyl ester acylhydrolase, 11-cis'' retinol-forming. This enzyme participates in retinol metabolism.
References
EC 3.1.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alpha-amino-acid%20esterase | The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction
an α-amino acid ester + H2O an α-amino acid + an alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is α-amino-acid-ester aminoacylhydrolase. This enzyme is also called α-amino acid ester hydrolase.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 3.1.1
Enzymes of known structure |
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