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https://en.wikipedia.org/wiki/Citrate%20CoA-transferase | In enzymology, a citrate CoA-transferase () is an enzyme that catalyzes the following chemical reaction:
acetyl-CoA + citrate acetate + (3S)-citryl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and citrate, whereas its two products are acetate and (3S)-citryl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:citrate CoA-transferase. This enzyme participates in citrate cycle (tca cycle).
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Coenzyme-B%20sulfoethylthiotransferase | In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as 2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreonine S-(2-sulfoethyl)thiotransferase is an enzyme that catalyzes the final step in the formation of methane. It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas on earth was produced. Ruminants (e.g. cows) produce methane because their rumens contain methanogenic prokaryotes (Archaea) that encode and express the set of genes of this enzymatic complex.
The enzyme has two active sites, each occupied by the nickel-containing F430 cofactor.
+ CoM-S-S-CoB + methane
The two substrates of this enzyme are 2-(methylthio)ethanesulfonate and N-(7-mercaptoheptanoyl)threonine 3-O-phosphate; its two products are CoM-S-S-CoB and methane. 3-Nitrooxypropanol inhibits the enzyme.
In some species, the enzyme reacts in reverse (a process called reverse methanogenesis), catalysing the anaerobic oxidation of methane, therefore removing it from the environment. Such organisms are methanotrophs.
This enzyme belongs to the family of transferases, specifically those transferring alkylthio groups.
This enzyme participates in folate biosynthesis.
Structure
Coenzyme-B sulfoethylthiotransferase is a multiprotein complex made up of a pair of identical halves. Each half is made up of three subunits: α, β and γ, also called McrA, Mcr |
https://en.wikipedia.org/wiki/Cortisol%20sulfotransferase | In enzymology, a cortisol sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + cortisol adenosine 3',5'-bisphosphate + cortisol 21-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and cortisol, whereas its two products are adenosine 3',5'-bisphosphate and cortisol 21-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:cortisol 21-sulfotransferase. Other names in common use include glucocorticosteroid sulfotransferase, and glucocorticoid sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine%20desulfurase | In enzymology, a cysteine desulfurase () is an enzyme that catalyzes the chemical reaction
L-cysteine + [enzyme]-cysteine L-alanine + [enzyme]-S-sulfanylcysteine
Thus, the two substrates of this enzyme are L-cysteine and [enzyme]-cysteine], whereas its two products are L-alanine and [enzyme]-S-sulfanylcysteine.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase. This enzyme participates in thiamine 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 2.8.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Desulfoglucosinolate%20sulfotransferase | In enzymology, a desulfoglucosinolate sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + desulfoglucotropeolin adenosine 3',5'-bisphosphate + glucotropeolin
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and desulfoglucotropeolin, whereas its two products are adenosine 3',5'-bisphosphate and glucotropeolin.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:desulfoglucosinolate sulfotransferase. Other names in common use include PAPS-desulfoglucosinolate sulfotransferase, 3'-phosphoadenosine-5'-phosphosulfate:desulfoglucosinolate, and sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Estrone%20sulfotransferase | Estrone sulfotransferase (EST) (), also known as estrogen sulfotransferase, is an enzyme that catalyzes the transformation of an unconjugated estrogen like estrone into a sulfated estrogen like estrone sulfate. It is a steroid sulfotransferase and belongs to the family of transferases, to be specific, the sulfotransferases, which transfer sulfur-containing groups. This enzyme participates in androgen and estrogen metabolism and sulfur metabolism.
Steroid sulfatase is an enzyme that catalyzes the reverse reaction, the transfer of a sulfate to an unconjugated estrogen.
Reaction
In enzymology, an EST is an enzyme that catalyzes the following chemical reaction:
3'-phosphoadenylyl sulfate + estrone adenosine 3',5'-bisphosphate + estrone 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and estrone, whereas its two products are adenosine 3',5'-bisphosphate and estrone 3-sulfate.
The enzyme also catalyzes the same reaction for estradiol, with estradiol sulfate as the product.
Types
Two enzymes have been identified that together are thought to represent estrone sulfotransferase (EST):
SULT1A1 (catalyzes the reactions estradiol to estradiol sulfate and, to a lesser extent than SULT1E1, estrone to estrone sulfate)
SULT1E1 (catalyzes the reactions estrone to estrone sulfate and estradiol to estradiol sulfate)
Function
Structure
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
Name |
https://en.wikipedia.org/wiki/Flavonol%203-sulfotransferase | In enzymology, a flavonol 3-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + flavonol adenosine 3',5'-bisphosphate + flavonol 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and a flavonol, whereas its two products are adenosine 3',5'-bisphosphate and flavonol 3-sulfate. A specific examples of a flavonol that can act as a substrate is quercetin.
This enzyme belongs to the family of transferases termed the sulfotransferases, which transfer sulfate groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:flavonol 3-sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formyl-CoA%20transferase | In enzymology, a formyl-CoA transferase () is an enzyme that catalyzes the chemical reaction
formyl-CoA + oxalate formate + oxalyl-CoA
Thus, the two substrates of this enzyme are formyl-CoA and oxalate, whereas its two products are formate and oxalyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is formyl-CoA:oxalate CoA-transferase. Other names in common use include formyl-coenzyme A transferase, and formyl-CoA oxalate CoA-transferase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.8.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Galactosylceramide%20sulfotransferase | In enzymology, a galactosylceramide sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + a galactosylceramide adenosine 3',5'-bisphosphate + a galactosylceramidesulfate
Thus, its two substrates are 3'-phosphoadenylyl sulfate and galactosylceramide, and its two products are adenosine 3',5'-bisphosphate and galactosylceramidesulfate.
It belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:galactosylceramide 3'-sulfotransferase. Other names in common use include GSase, 3'-phosphoadenosine-5'-phosphosulfate-cerebroside sulfotransferase, galactocerebroside sulfotransferase, galactolipid sulfotransferase, glycolipid sulfotransferase, and glycosphingolipid sulfotransferase. This enzyme participates in sphingolipid metabolism.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutaconate%20CoA-transferase | In enzymology, a glutaconate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + (E)-glutaconate acetate + glutaconyl-1-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and (E)-glutaconate, whereas its two products are acetate and glutaconyl-1-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:(E)-glutaconate CoA-transferase. This enzyme participates in styrene degradation and butanoate metabolism.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycochenodeoxycholate%20sulfotransferase | In enzymology, a glycochenodeoxycholate sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + glycochenodeoxycholate adenosine 3',5'-bisphosphate + glycochenodeoxycholate 7-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and glycochenodeoxycholate, whereas its two products are adenosine 3',5'-bisphosphate and glycochenodeoxycholate 7-sulfate.
Nomenclature
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase. Other names in common use include bile acid:3'-phosphoadenosine-5'-phosphosulfate sulfotransferase, bile acid:PAPS:sulfotransferase, and BAST.
References
Further reading
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28heparan%20sulfate%29-glucosamine%203-sulfotransferase%201 | In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 1 () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenosine 3',5'-bisphosphate and heparan sulfate-glucosamine 3-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase. Other names in common use include heparin-glucosamine 3-O-sulfotransferase, 3'-phosphoadenylyl-sulfate:heparin-glucosamine 3-O-sulfotransferase, glucosaminyl 3-O-sulfotransferase, heparan sulfate D-glucosaminyl 3-O-sulfotransferase, and isoform/isozyme 1 (3-OST-1, HS3ST1). This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.8.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Honda%20FCX | The Honda FCX (commonly referred to as Fuel Cell eXperimental) is a family of hydrogen fuel cell automobiles manufactured by Honda.
The Honda FCX and Toyota FCHV, which began leasing on December 2, 2002, became the world's first government-certified commercial hydrogen fuel cell vehicles.
As of March 2007, there are more than twenty Honda FCX vehicles in the hands of customers, including the state of New York, cities of Las Vegas, Chula Vista, San Francisco and the South Coast Air Quality Management District in three different American states.
Limited marketing of a latest fuel cell vehicle named FCX Clarity, based on the 2007 concept model, began on June 19, 2008 in Japan and the United States. Honda believes it could start mass-producing the next model evolved from the FCX concept by 2018.
1999 FCX concept and prototypes
The first prototype FCX is a four-door, four-seat vehicle that was launched in 1999. Dimensions are: length 4165 mm, width 1760 mm and height 1645 mm. The fuel cell was a PEFC (proton exchange membrane) manufactured by Ballard Power Systems. The fuel cell had power output of 78 kW.
The engine has a maximum output of 80 horsepower (60 kilowatts), torque of and has an EPA certified range of 170 miles.
The first vehicles were delivered on December 2, 2002, in the USA (City of Los Angeles) and Japan.
1999 September
Honda FCX-V1: Hydrogen vehicle model
Honda FCX-V2: Methanol-fuel cell model
2000 September
Honda FCX-V3: Supercapacitor model, began t |
https://en.wikipedia.org/wiki/%28heparan%20sulfate%29-glucosamine%203-sulfotransferase%202 | In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 2 () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenine 3',5'-bis-phosphate and heparan sulfate-glucosamine 3-sulfate.
This enzyme belongs to the family of transferences, specifically the transformer, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphorylation-sulfate:[heparin sulfate]-glucose 3-nontransferable. Other names in common use include glucose 3-O-nontransferable, heparin sulfate D-glucose 3-O-nontransferable, and formalism/isomerism 2 (3-OAT-2, HST). This enzyme participates in heparan sulfate biosynthesis and glycogen structures - biosynthesis 1.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28heparan%20sulfate%29-glucosamine%203-sulfotransferase%203 | In enzymology, a [heparan sulfate]-glucosamine 3-sulfotransferase 3 () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenosine 3',5'-bisphosphate and heparan sulfate-glucosamine 3-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase. This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28heparan%20sulfate%29-glucosamine%20N-sulfotransferase | In enzymology, a [heparan sulfate]-glucosamine N-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and heparan sulfate-glucosamine, whereas its two products are adenosine 3',5'-bisphosphate and heparan sulfate-N-sulfoglucosamine.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine N-sulfotransferase. Other names in common use include heparin N-sulfotransferase, 3'-phosphoadenylylsulfate:N-desulfoheparin sulfotransferase, PAPS:N-desulfoheparin sulfotransferase, PAPS:DSH sulfotransferase, N-HSST, N-heparan sulfate sulfotransferase, heparan sulfate N-deacetylase/N-sulfotransferase, heparan sulfate 2-N-sulfotransferase, heparan sulfate N-sulfotransferase, heparan sulfate sulfotransferase, N-desulfoheparin sulfotransferase, desulfoheparin sulfotransferase, 3'-phosphoadenylyl-sulfate:N-desulfoheparin N-sulfotransferase, heparitin sulfotransferase, and 3'-phosphoadenylyl-sulfate:heparitin N-sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Keratan%20sulfotransferase | In enzymology, a keratan sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + keratan adenosine 3',5'-bisphosphate + keratan 6'-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and keratan, whereas its two products are adenosine 3',5'-bisphosphate and keratan 6'-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:keratan 6'-sulfotransferase. Other names in common use include 3'-phosphoadenylyl keratan sulfotransferase, keratan sulfate sulfotransferase, and 3'-phosphoadenylylsulfate:keratan sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Lipoyl%20synthase | Lipoyl synthase is an enzyme that belongs to the radical SAM (S-adenosyl methionine) family. Within the radical SAM superfamily, lipoyl synthase is in a sub-family of enzymes that catalyze sulfur insertion reactions. The enzymes in this subfamily differ from general radical SAM enzymes, as they contain two 4Fe-4S clusters. From these clusters, the enzymes obtain the sulfur groups that will be transferred onto the corresponding substrates. This particular enzyme participates in the final step of lipoic acid metabolism, transferring two sulfur atoms from its 4Fe-4S cluster onto the protein N6-(octanoyl)lysine through radical generation. This enzyme is usually localized to the mitochondria. Two organisms that have been extensively studied with regards to this enzyme are Escherichia coli and Mycobacterium tuberculosis. It is currently being studied in other organisms including yeast, plants, and humans.
Nomenclature
The systematic name of this enzyme class is protein N6-(octanoyl)lysine:sulfur sulfurtransferase. Other names in common use include:
LS
LipA
lipoate synthase
protein 6-N-(octanoyl)lysine:sulfur sulfurtransferase.
Structure
The sequence length of M. tuberculosis lipoyl synthase is approximately 331 amino acids. The structure is composed of 11 α-helices and 7 β sheets, with multiple loop structures connecting the other components. The two [4Fe-4S] clusters are located within the structure, appearing in three-dimensional cubic shape. A molecule of DTV ((2S,3S)- |
https://en.wikipedia.org/wiki/L-seryl-tRNASec%20selenium%20transferase | In enzymology, a L-seryl-tRNASec selenium transferase () is an enzyme that catalyzes the chemical reaction
L-seryl-tRNASec + selenophosphate L-selenocysteinyl-tRNASec + phosphate
Thus, the two substrates of this enzyme are L-seryl-tRNASec and selenophosphate, whereas its two products are L-selenocysteinyl-tRNASec and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring selenium-containing groups selenotransferases. The systematic name of this enzyme class is selenophosphate:L-seryl-tRNASec selenium transferase. Other names in common use include L-selenocysteinyl-tRNASel synthase, L-selenocysteinyl-tRNASec synthase selenocysteine synthase, cysteinyl-tRNASec-selenium transferase, and cysteinyl-tRNASec-selenium transferase. This enzyme participates in selenoamino acid metabolism. It employs one cofactor, pyridoxal phosphate.
References
EC 2.9.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pterygium | Pterygium (plural pterygia or pterygiums) refers to any wing-like triangular membrane occurring in the neck, eyes, knees, elbows, ankles or digits.
The term comes from the Greek word pterygion meaning "wing".
Types
Popliteal pterygium syndrome, a congenital condition affecting the face, limbs, or genitalia but named after the wing-like structural anomaly behind the knee
Pterygium (eye) or surfer's eye, a growth on the cornea of the eye
Pterygium colli or webbed neck, a congenital skin fold of the neck down to the shoulders
Pterygium inversum unguis or ventral pterygium, adherence of the distal portion of the nailbed to the ventral surface of the nail plate
Pterygium unguis or dorsal pterygium, scarring between the proximal nail fold and matrix
Pterygium of the eye
A pterygium reduces the vision in several ways:
Distortion of the corneal optics. This begins usually when the pterygium is greater than 2mm from the corneal edge (limbus).
Disruption of the tear film. The tear film is the first lens in the eye. Pterygia are associated with eyelid inflammation, called Blepharitis.
Growth over the corneal centre, which leads to dramatic reduction of vision.
Induced anterior corneal scarring, which often remains after surgical removal.
A pterygium of the eye grows very slowly. Usually it takes several years or decades to progress.
Surgical removal
Indications for surgery, in order of decreasing importance:
Growth over the corneal centre.
Reduced vision du |
https://en.wikipedia.org/wiki/Afterhyperpolarization | Afterhyperpolarization, or AHP, is the hyperpolarizing phase of a neuron's action potential where the cell's membrane potential falls below the normal resting potential. This is also commonly referred to as an action potential's undershoot phase. AHPs have been segregated into "fast", "medium", and "slow" components that appear to have distinct ionic mechanisms and durations. While fast and medium AHPs can be generated by single action potentials, slow AHPs generally develop only during trains of multiple action potentials.
During single action potentials, transient depolarization of the membrane opens more voltage-gated K+ channels than are open in the resting state, many of which do not close immediately when the membrane returns to its normal resting voltage. This can lead to an "undershoot" of the membrane potential to values that are more polarized ("hyperpolarized") than was the original resting membrane potential. Ca2+-activated K+ channels that open in response to the influx of Ca2+ during the action potential carry much of the K+ current as the membrane potential becomes more negative. The K+ permeability of the membrane is transiently unusually high, driving the membrane voltage VM even closer to the K+ equilibrium voltage EK. Hence, hyperpolarization persists until the membrane K+ permeability returns to its usual value.
Medium and slow AHP currents also occur in neurons. The ionic mechanisms underlying medium and slow AHPs are not yet well understood, but may a |
https://en.wikipedia.org/wiki/Lyonsite | Lyonsite (Cu3Fe+34(VO4)6) is a rare black vanadate mineral that is opaque with a metallic lustre. It crystallizes in the orthorhombic crystal system. Lyonsite often occurs as small tabular typically well formed crystals. Lyonsite has a good cleavage and a dark gray streak.
Lyonsite occurs as a sublimate in volcanic fumaroles. It is often associated with howardevansite and thenardite. It was first described in 1987 for an occurrence on the Izalco volcano, El Salvador. It was named for mineralogist John Bartholomew Lyons (1916–1998) of Dartmouth College. It has also been reported from a mine dump in the Lichtenberg Absetzer Mine of Thuringia, Germany.
References
Copper(II) minerals
Iron(III) minerals
Vanadate minerals
Orthorhombic minerals
Minerals in space group 62
Minerals described in 1987 |
https://en.wikipedia.org/wiki/Conservation%20grazing | Conservation grazing or targeted grazing is the use of semi-feral or domesticated grazing livestock to maintain and increase the biodiversity of natural or semi-natural grasslands, heathlands, wood pasture, wetlands and many other habitats. Conservation grazing is generally less intensive than practices such as prescribed burning, but still needs to be managed to ensure that overgrazing does not occur. The practice has proven to be beneficial in moderation in restoring and maintaining grassland and heathland ecosystems. The optimal level of grazing will depend on the goal of conservation, and different levels of grazing, alongside other conservation practices, can be used to induce the desired results.
History
For historic grasslands, grazing animals, herbivores, were a crucial part of the ecosystem. When grazers are removed, historically grazed lands may show a decline in both the density and the diversity of the vegetation. The history of the land may help ecologists and conservationists determine the best approach to a conservation project.
Historic threats to grasslands began with land conversion to crop fields. This shifted to improper land management techniques and more recently to the spread of woody plants due to a lack of management and to climate change.
Conservation grazing in practice
Intensive grazing maintains an area as a habitat dominated by grasses and small shrubs, largely preventing ecological succession to forest.
Extensive grazing also treats habita |
https://en.wikipedia.org/wiki/Discovery%20and%20development%20of%20ACE%20inhibitors | The discovery of an orally inactive peptide from snake venom established the important role of angiotensin converting enzyme (ACE) inhibitors in regulating blood pressure. This led to the development of captopril, the first ACE inhibitor. When the adverse effects of captopril became apparent new derivates were designed. Then after the discovery of two active sites of ACE: N-domain and C-domain, the development of domain-specific ACE inhibitors began.
Development of first generation ACE inhibitors
The development of the nonapeptide teprotide (Glu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro), which was originally isolated from the venom of the Brazilian pit viper Bothrops jararaca, greatly clarified the importance of ACE in hypertension. However, its lack of oral activity limited its therapeutic utility.
L-benzylsuccinic acid (2(R)-benzyl-3-carboxypropionic acid) was described to be the most potent inhibitor of carboxypeptidase A in the early 1980s. The authors referred to it as a by-product analog and it was proposed to bind to the active site of carboxypeptidase A via succinyl carboxyl group and a carbonyl group. Their findings established that L-benzylsuccinic acid is bound at a single locus at the active site of carboxypeptidase A. The authors discussed but dismissed the suggestion that the carboxylate function might bind to the catalytically functional zinc ion present at the active site. Later however this was found to be the case.
Drug design of captopril (sulfhydrils)
Over 2000 |
https://en.wikipedia.org/wiki/Protease-activated%20receptor%202 | Protease activated receptor 2 (PAR2) also known as coagulation factor II (thrombin) receptor-like 1 (F2RL1) or G-protein coupled receptor 11 (GPR11) is a protein that in humans is encoded by the F2RL1 gene. PAR2 modulates inflammatory responses, obesity, metabolism, cancers and acts as a sensor for proteolytic enzymes generated during infection. In humans, we can find PAR2 in the stratum granulosum layer of epidermal keratinocytes. Functional PAR2 is also expressed by several immune cells such as eosinophils, neutrophils, monocytes, macrophages, dendritic cells, mast cells and T cells.
Gene
The F2RL1 gene contains two exons and is widely expressed in human tissues. The predicted protein sequence is 83% identical to the mouse receptor sequence.
Mechanism of activation
PAR2 is a member of the large family of 7-transmembrane receptors that couple to guanosine-nucleotide-binding proteins. PAR2 is also a member of the protease-activated receptor family. PAR2 is activated by several different endogenous and exogenous proteases. It is activated by proteolytic cleavage of its extracellular amino terminus between arginine and serine. The newly exposed N-terminus serves as tethered activation ligand, which binds a conserved region on extracellular loop 2 (ECL2) and activates the receptor. These receptors can also be activated non-protealytically, by exogenous peptide sequences that mimic the final amino acids of the tethered ligand, or by other proteases at cleavage sites that |
https://en.wikipedia.org/wiki/Dual%20EC%20DRBG | Dual_EC_DRBG (Dual Elliptic Curve Deterministic Random Bit Generator) is an algorithm that was presented as a cryptographically secure pseudorandom number generator (CSPRNG) using methods in elliptic curve cryptography. Despite wide public criticism, including the public identification of the possibility that the National Security Agency put a backdoor into a recommended implementation, it was for seven years one of four CSPRNGs standardized in NIST SP 800-90A as originally published circa June 2006, until it was withdrawn in 2014.
Weakness: a potential backdoor
Weaknesses in the cryptographic security of the algorithm were known and publicly criticised well before the algorithm became part of a formal standard endorsed by the ANSI, ISO, and formerly by the National Institute of Standards and Technology (NIST). One of the weaknesses publicly identified was the potential of the algorithm to harbour a cryptographic backdoor advantageous to those who know about it—the United States government's National Security Agency (NSA)—and no one else. In 2013, The New York Times reported that documents in their possession but never released to the public "appear to confirm" that the backdoor was real, and had been deliberately inserted by the NSA as part of its Bullrun decryption program. In December 2013, a Reuters news article alleged that in 2004, before NIST standardized Dual_EC_DRBG, NSA paid RSA Security $10 million in a secret deal to use Dual_EC_DRBG as the default in the RS |
https://en.wikipedia.org/wiki/Malonate%20CoA-transferase | In enzymology, a malonate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + malonate acetate + malonyl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and malonate, whereas its two products are acetate and malonyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:malonate CoA-transferase. This enzyme is also called malonate coenzyme A-transferase. This enzyme participates in beta-alanine metabolism and propanoate metabolism.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Oxalate%20CoA-transferase | In enzymology, an oxalate CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + oxalate succinate + oxalyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and oxalate, whereas its two products are succinate and oxalyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:oxalate CoA-transferase. Other names in common use include succinyl-beta-ketoacyl-CoA transferase, and oxalate coenzyme A-transferase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Petromyzonol%20sulfotransferase | In enzymology, a petromyzonol sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + 5alpha-cholan-3alpha,7alpha,12alpha,24-tetrol adenosine 3',5'-bisphosphate + 5alpha-cholan-3alpha,7alpha,12alpha-triol 24-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and 5alpha-cholan-3alpha,7alpha,12alpha,24-tetrol, whereas its two products are adenosine 3',5'-bisphosphate and 5alpha-cholan-3alpha,7alpha,12alpha-triol 24-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:5alpha-cholan-3alpha,7alpha,12alpha,24-te trol sulfotransferase. This enzyme is also called PZ-SULT.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Propionate%20CoA-transferase | In enzymology, a propionate CoA-transferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + propanoate acetate + propanoyl-CoA
Thus, the two substrates of this enzyme are acetyl-CoA and propanoate, whereas its two products are acetate and propanoyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:propanoate CoA-transferase. Other names in common use include propionate coenzyme A-transferase, propionate-CoA:lactoyl-CoA transferase, propionyl CoA:acetate CoA transferase, and propionyl-CoA transferase. This enzyme participates in 3 metabolic pathways: pyruvate metabolism, propanoate metabolism, and styrene degradation.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Psychosine%20sulfotransferase | In enzymology, a psychosine sulfotransferase () is an enzyme that catalyzes the chemical reaction:
3'-phosphoadenylyl sulfate + galactosylsphingosine adenosine 3',5'-bisphosphate + psychosine sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and galactosylsphingosine, whereas its two products are adenosine 3',5'-bisphosphate and psychosine sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:galactosylsphingosine sulfotransferase. Other names in common use include PAPS:psychosine sulphotransferase, and 3'-phosphoadenosine 5'-phosphosulfate-psychosine sulphotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Quercetin-3%2C3%27-bissulfate%207-sulfotransferase | In enzymology, a quercetin-3,3'-bissulfate 7-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + quercetin 3,3'-bissulfate adenosine 3',5'-bisphosphate + quercetin 3,7,3'-trisulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and quercetin 3,3'-bissulfate, whereas its two products are adenosine 3',5'-bisphosphate and quercetin 3,7,3'-trissulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:quercetin-3,3'-bissulfate 7-sulfotransferase. Other names in common use include flavonol 7-sulfotransferase, 7-sulfotransferase, and PAPS:flavonol 3,3'/3,4'-disulfate 7-sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure
Quercetin |
https://en.wikipedia.org/wiki/Integrin%20alpha%206 | Integrin alpha-6 is a protein that in humans is encoded by the ITGA6 gene.
Function
The ITGA6 protein product is the integrin alpha chain alpha 6. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. For example, alpha 6 may combine with beta 4 in the integrin referred to as TSP180, or with beta 1 in the integrin VLA-6. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling. Two transcript variants encoding different isoforms have been found for this gene. Specific loss of this integrin chain in the intestinal epithelium, and thus of their hemidesmosomes, induces long-standing colitis and infiltrating adenocarcinomas.
Interactions
ITGA6 has been shown to interact with TSPAN4 and GIPC1.
See also
Cluster of differentiation
Integrins
References
Further reading
External links
ITGA6 Info with links in the Cell Migration Gateway
Integrins
Clusters of differentiation |
https://en.wikipedia.org/wiki/Scymnol%20sulfotransferase | In enzymology, a scymnol sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-Phosphoadenosine-5'-phosphosulfate + 5beta-scymnol adenosine 3',5'-bisphosphate + 5beta-scymnol sulfate
Thus, the two substrates of this enzyme are 3'-Phosphoadenosine-5'-phosphosulfate and 5beta-scymnol, whereas its two products are adenosine 3',5'-bisphosphate and 5beta-scymnol sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-Phosphoadenosine-5'-phosphosulfate:5beta-scymnol sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Strain%20rate | In mechanics and materials science, strain rate is the time derivative of strain of a material. Strain rate has dimension of inverse time and SI units of inverse second, s−1 (or its multiples).
The strain rate at some point within the material measures the rate at which the distances of adjacent parcels of the material change with time in the neighborhood of that point. It comprises both the rate at which the material is expanding or shrinking (expansion rate), and also the rate at which it is being deformed by progressive shearing without changing its volume (shear rate). It is zero if these distances do not change, as happens when all particles in some region are moving with the same velocity (same speed and direction) and/or rotating with the same angular velocity, as if that part of the medium were a rigid body.
The strain rate is a concept of materials science and continuum mechanics that plays an essential role in the physics of fluids and deformable solids. In an isotropic Newtonian fluid, in particular, the viscous stress is a linear function of the rate of strain, defined by two coefficients, one relating to the expansion rate (the bulk viscosity coefficient) and one relating to the shear rate (the "ordinary" viscosity coefficient). In solids, higher strain rates can often cause normally ductile materials to fail in a brittle manner.
Definition
The definition of strain rate was first introduced in 1867 by American metallurgist Jade LeCocq, who defined it as "th |
https://en.wikipedia.org/wiki/Galectin-1 | Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.
Gene and protein
LGALS1 contains four exons. The galectin-1 protein is 135 amino acids in length and highly conserved across species. It can be found in the nucleus, the cytoplasm, the cell surface and in the extracellular space. Galectins in general lack a traditional signal sequence, but are still secreted across the plasma membrane. This non-traditional secretion requires a functional glycan binding site. Galectin 1 contains a single carbohydrate recognition domain through which it can bind glycans both as a monomer and as a homodimer. Dimers are non-covalently bound and will spontaneously disassociate in low concentration. Galectin 1 does not bind glycans when oxidized. Having 6 cysteine residues, the oxidation state has a significant effect on the protein structure. The oxidized form is reported to have alternative functions not involving carbohydrate binding.
Function
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 may act as an autocrine negative growth factor that regulates cell proliferation. Galectin-1 expression in Hodgkin Lymphoma has also been shown to mediate immunosuppression of CD8+ T-cells.
It has been linked to the inflammatory process in HIV individuals, and some research suggest that Gal-1 could be related to the HIV-1 latency.
Role in pregnancy
Galectin-1 is thought to play a role in cre |
https://en.wikipedia.org/wiki/Studentized%20range%20distribution | In probability and statistics, studentized range distribution is the continuous probability distribution of the studentized range of an i.i.d. sample from a normally distributed population.
Suppose that we take a sample of size n from each of k populations with the same normal distribution N(μ, σ2) and suppose that is the smallest of these sample means and is the largest of these sample means, and suppose s² is the pooled sample variance from these samples. Then the following statistic has a Studentized range distribution.
Definition
Probability density function
Differentiating the cumulative distribution function with respect to q gives the probability density function.
Note that in the outer part of the integral, the equation
was used to replace an exponential factor.
Cumulative distribution function
The cumulative distribution function is given by
Special cases
If k is 2 or 3, the studentized range probability distribution function can be directly evaluated, where is the standard normal probability density function and is the standard normal cumulative distribution function.
When the degrees of freedom approaches infinity the studentized range cumulative distribution can be calculated for any k using the standard normal distribution.
Applications
Critical values of the studentized range distribution are used in Tukey's range test.
The studentized range is used to calculate significance levels for results obtained by data mining, where one selectively seeks ex |
https://en.wikipedia.org/wiki/Geoffrey%20%28name%29 | Geoffrey is an English and German masculine given name. It is generally considered the Anglo-Norman form of the Germanic compound 'god' and 'peace'. It is a derivative of Dutch Godfried, German Gottfried and Old English Gotfrith and Godfrith.
Alexander Macbain considered it as being found in the Gaelic and Welsh forms; potentially before or contemporary to the Anglo-Saxon, with the examples of Goraidh, Middle Gaelic Gofraig (1467 MS.), Godfrey (do.), Irish Gofraidh (F.M.), Middle Irish Gothfrith, Gofraig (Tigernach, 989), Early Irish Gothfraid (Lib. Lein.), E. Welsh Gothrit (Ann. Camb.). Macbain suggested these Celtic forms of the name were closer related to the Anglo-Saxon Godefrid than the Norse Goðröðr, Gudrød or Góröðr; however he does not elaborate further on the origin or relation.
The form as 'Geoffrey' was probably introduced to Norman England.
It was also Anglicised as Jeffrey later after the name became more popular after the likes of President Jefferson. Popularity of the name declined after the medieval period, but it was revived in modern England and the British Empire at large. Modern hypocorisms include Geoff or Jeff.
Jeffrey and its variants are found as surnames, usually ending in -s (e.g. Jefferies, Jaffrays); The surname Jefferson is also a patronymic version of the given name.
Etymology
The Old French form of the name was Geoffrei ([dʒɔfrej]), which developed into West Middle French Geoffrey and East Middle French Geoffroy.
Latinised forms include |
https://en.wikipedia.org/wiki/PAR3 | PAR3 may refer to:
Parchive, an error correction system for computer files. The third version is known as PAR3.
Protease activated receptor 3, a G-protein coupled receptor protein
Pseudoautosomal region 3, a region of homologous sequences between the human X and Y chromosome
Partitioning defective 3 homolog, a protein that in humans is encoded by the PARD3 gene
See also
3PAR |
https://en.wikipedia.org/wiki/Dehydroacetic%20acid | Dehydroacetic acid is an organic compound which has several industrial applications. The compound is classified as a pyrone derivative. It presents as an odorless, colorless to white crystalline powder, almost insoluble in water and moderately soluble in most organic solvents.
Preparation
It is prepared by the base-catalysed dimerization of diketene. Commonly used organic bases include imidazole, DABCO, and pyridine.
Uses
Industrially, dehydroacetic acid has several uses which include the following:
as a fungicide and bactericide. The sodium salt, sodium dehydroacetate, is often used in place of dehydroacetic acid because of its greater solubility in water.
as a food preservative to prevent pickle bloating in squash and strawberries. When used as a food additive, dehydroacetic acid is referred to using the International Numbering System for Food Additives or E number 265.
as a plasticizer in synthetic resins.
as an antienzyme in toothpastes.
as a precursor for dimethyl-4-pyridones. The compounds are synthesized when dehydroacetic acid is exposed to aqueous solutions containing primary amines.
References
Fungicides
4-Pyrones |
https://en.wikipedia.org/wiki/Sodium%20malate | Sodium malate is a compound with formula Na2(C2H4O(COO)2). It is the sodium salt of malic acid. As a food additive, it has the E number E350.
Properties
Sodium malate is an odorless white crystalline powder. It is freely soluble in water.
Use
It is used as an acidity regulator and flavoring agent. It tastes similar to sodium chloride (table salt).
References
Malates
Organic sodium salts
E-number additives |
https://en.wikipedia.org/wiki/Sulazepam | Sulazepam is a benzodiazepine derivative. It is the thioamide derivative of diazepam. It is metabolised into diazepam, desmethyldiazepam and oxydiazepam. It has sedative, muscle relaxant, hypnotic, anticonvulsant and anxiolytic properties like those of other benzodiazepines. It was never marketed.
Synthesis
Treatment of diazepam with phosphorus pentasulfide produces the corresponding thionamide, sulazepam.
See also
Uldazepam
References
Benzodiazepines
Chloroarenes
GABAA receptor positive allosteric modulators
Thioamides |
https://en.wikipedia.org/wiki/Menitrazepam | Menitrazepam is a drug which is a benzodiazepine derivative. It is similar in structure to tetrazepam and nimetazepam, with the 7-chloro group of tetrazepam replaced by nitro. It is a hypnotic agent used in the treatment of insomnia, and therefore has strong sedative, anticonvulsant, muscle relaxant, and anxiolytic actions like those of other hypnotic benzodiazepines. Menitrazepam is a good oral hypnotic agent, however, delay in the time for peak plasma levels to reach their maximum brings into question the benefit of menitrazepam for the treatment of insomnia when compared to other hypnotics. Typically, the sleep inducing properties of hypnotics occur within 0.5 hours. In some cases, as with temazepam and nitrazepam, strong hypnotic effects can be felt 15 to 20 minutes after oral ingestion.
See also
Tetrazepam
References
GABAA receptor positive allosteric modulators
Lactams
Nitrobenzodiazepines
Cyclohexenes |
https://en.wikipedia.org/wiki/Uldazepam | Uldazepam is a drug which is a benzodiazepine derivative. It has sedative and anxiolytic effects similar to those of other benzodiazepines.
Synthesis
Thio thionamide is even more prone to amidine formation than the lactam itself.
Reaction of thionamide (2) with O-allyl-hydroxylamine gave the oximino (3) uldazepam.
See also
Benzodiazepine
References
Allyl compounds
Benzodiazepines
Chloroarenes
GABAA receptor positive allosteric modulators |
https://en.wikipedia.org/wiki/Trace%20table | A trace table is a technique used to test algorithms in order to make sure that no logical errors occur while the calculations are being processed. The table usually takes the form of a multi-column, multi-row table; With each column showing a variable, and each row showing each number input into the algorithm and the subsequent values of the variables.
Trace tables are typically used in schools and colleges when teaching students how to program. They can be an essential tool in teaching students how certain calculations works and the systematic process that is occurring when the algorithm is executed. They can also be useful for debugging applications, helping the programmer to easily detect what error is occurring, and why it may be occurring.
Example
int i, x = 0;
for (i = 1; i <= 10; i++)
{
x = i * 2;
}
This example shows the systematic process that takes place whilst the algorithm is processed. The initial value of x is zero, but i, although defined, has not been assigned a value. Thus, its initial value is unknown. As we execute the program, line by line, the values of i and x change, reflecting each statement of the source code in execution. Their new values are recorded in the trace table. When i reaches the value of 11 because of the i++ statement in the for definition, the comparison i <= 10 evaluates to false, thus halting the loop. As we also reached the end of the program, the trace table also ends.
See also
Algorithms
Programming languages
Debuggi |
https://en.wikipedia.org/wiki/Elfazepam | Elfazepam is a drug which is a benzodiazepine derivative. Presumably it has sedative and anxiolytic actions like those of other benzodiazepines.
Orexigenic properties in animals. The mechanism for increasing feed intake is not clear and has been subject of investigation. It has been found that elfazepam suppresses gastric acid secretion.
Synthesis
Benzophenone derivative 1 is reacted with a glycine equivalent masked as an oxazolidine-2,5-dione 2 to give the final product 3 Elfazepam.
References
Benzodiazepines
Chloroarenes
GABAA receptor positive allosteric modulators
Lactams
Fluoroarenes |
https://en.wikipedia.org/wiki/Meclonazepam | Meclonazepam ((S)-3-methylclonazepam) was discovered by a team at Hoffmann-La Roche in the 1970s and is a drug which is a benzodiazepine derivative similar in structure to clonazepam. It has sedative and anxiolytic actions like those of other benzodiazepines, and also has anti-parasitic effects against the parasitic worm Schistosoma mansoni.
Meclonazepam was never used as medicine and instead appeared online as a designer drug.
Legal Issues
United Kingdom
In the UK, meclonazepam has been classified as a Class C drug by the May 2017 amendment to The Misuse of Drugs Act 1971 along with several other designer benzodiazepine drugs.
See also
3-Hydroxyphenazepam
Desmethylflunitrazepam
Nifoxipam
Oxazepam
Phenazepam
Ro05-4082
SH-I-048A
References
Further reading
Chloroarenes
Designer drugs
GABAA receptor positive allosteric modulators
Lactams
Nitrobenzodiazepines |
https://en.wikipedia.org/wiki/Chester%20Ittner%20Bliss | Chester Ittner Bliss (February 1, 1899 – March 14, 1979) was primarily a biologist, who is best known for his contributions to statistics. He was born in Springfield, Ohio in 1899 and died in 1979. He was the first secretary of the International Biometric Society.
Academic qualifications
Bachelor of Arts in Entomology from Ohio State University, 1921
Master of Arts from Columbia University, 1922
PhD from Columbia University, 1926
Remarkably, his statistical knowledge was largely self-taught and developed according to the problems he wanted to solve (Cochran & Finney 1979).
Nevertheless, in 1942 he was elected as a Fellow of the American Statistical Association.
Major contributions
The idea of the probit function was published by Bliss in a 1934 article in Science on how to treat data such as the percentage of a pest killed by a pesticide. Bliss proposed transforming the percentage killed into a "probability unit" (or "probit").
Arguably his most important contribution was the development, with Ronald Fisher, of an iterative approach to finding maximum likelihood estimates in the probit method of bioassay. Additional contributions in biological assay were work on the analysis of time-mortality data and of slope-ratio assays (Cochran & Finney 1979).
Bliss introduced the word rankit, meaning an expected normal order statistic.
References
Citations
Sources
C. I. Bliss (1935) The calculation of the dosage-mortality curve, Annals of Applied Biology 22, 134–167. (include |
https://en.wikipedia.org/wiki/Girisopam | Girisopam (GYKI-51189, EGIS-5810) is a drug which is a 2,3-benzodiazepine derivative, related to tofisopam and zometapine. It has selective anxiolytic action with no sedative, anticonvulsant or muscle relaxant effects.
Synthesis
Henry reaction between Veratraldehyde [120-14-9] (1) and nitroethane gives 1,2-Dimethoxy-4-(2-nitropropenyl)benzene [122-47-4] (2). Treatment with iron and muriatic acid in the presence of iron trichloride catalyst gives 3,4-Dimethoxyphenylacetone [776-99-8] (3). The reduction of the ketone with sodium borohydride gives 1-(3,4-Dimethoxyphenyl)-2-propanol [19578-92-8] (4). Treatment with formaldehyde in acid gives 6,7-dimethoxy-3-methyl-1H-isochromene, CID:57074411 (5). Oxidation by chromium trichloride gives 3-Methyl-6,7-Dimethoxyisocoumarin, CID:12349213 (6). Grignard reaction with 1-Bromo-3-Chlorobenzene [108-37-2] (7) gives (8). Treatment with Perchloric acid leads to 1-(3-chlorophenyl)-3-methyl 6,7-dimethoxy-2-benzopyrylium perchlorate CID:14502385 (9).
The reaction between (9) and hydrazine hydrate (10) in methanol solvent gives girisopam (11).
See also
Benzodiazepine
References
Benzodiazepines
Chlorobenzenes
Phenol ethers |
https://en.wikipedia.org/wiki/List%20of%20Grand%20Slam%20girls%27%20doubles%20champions | List of Girls' Doubles Junior Grand Slam tournaments tennis champions:
Champions by year
Statistics
Most Grand Slam doubles titles
Note: when a tie, the person to reach the mark first is listed first.
Three titles in a single season
Surface Slam
Players who won Grand Slam titles on clay, grass and hard courts in a calendar year.
Channel Slam
Players who won the French Open-Wimbledon double.
Sources
ITF Australian Open
ITF Roland Garros
ITF Wimbledon
ITF US Open
References
See also
List of Grand Slam girls' singles champions
List of Grand Slam boys' singles champions
List of Grand Slam boys' doubles champions
girls
Grand Slam
Girls |
https://en.wikipedia.org/wiki/SPP1 | SPP1 or SPP-1 may refer to:
SPP-1 underwater pistol, a USSR firearm made for Soviet frogmen
Secreted phosphoprotein 1, a human gene product
Suppressor of Pericarp Pigmentation 1, a maize gene implied in the phlobaphene metabolic pathway |
https://en.wikipedia.org/wiki/Triflubazam | Triflubazam is a drug which is a 1,5-benzodiazepine derivative, related to clobazam. It has sedative and anxiolytic effects, with a long half-life and duration of action.
See also
Benzodiazepine
Clobazam
CP-1414S
Triflunordazepam
References
Benzodiazepines
GABAA receptor positive allosteric modulators
Lactams
Trifluoromethyl compounds |
https://en.wikipedia.org/wiki/Quercetin-3-sulfate%203%27-sulfotransferase | In enzymology, a quercetin-3-sulfate 3'-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + quercetin 3-sulfate adenosine 3',5'-bisphosphate + quercetin 3,3'-bissulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and quercetin 3-sulfate, whereas its two products are adenosine 3',5'-bisphosphate and quercetin 3,3'-bissulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 3'-sulfotransferase. Other names in common use include flavonol 3'-sulfotransferase, 3'-Sulfotransferase, and PAPS:flavonol 3-sulfate 3'-sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure
Quercetin |
https://en.wikipedia.org/wiki/Quercetin-3-sulfate%204%27-sulfotransferase | In enzymology, a quercetin-3-sulfate 4'-sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + quercetin 3-sulfate adenosine 3',5'-bisphosphate + quercetin 3,4'-bissulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and quercetin 3-sulfate, whereas its two products are adenosine 3',5'-bisphosphate and quercetin 3,4'-bissulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:quercetin-3-sulfate 4'-sulfotransferase. Other names in common use include flavonol 4'-sulfotransferase, and PAPS:flavonol 3-sulfate 4'-sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure
Quercetin |
https://en.wikipedia.org/wiki/Renilla-luciferin%20sulfotransferase | In enzymology, a Renilla-luciferin sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + Renilla luciferin adenosine 3',5'-bisphosphate + luciferyl sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and Renilla luciferin, whereas its two products are adenosine 3',5'-bisphosphate and luciferyl sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:Renilla luciferin sulfotransferase. Other names in common use include luciferin sulfotransferase, luciferin sulfokinase, luciferin sulfokinase (3'-phosphoadenylyl sulfate:luciferin, and sulfotransferase).
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Steroid%20sulfotransferase | In enzymology, a steroid sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + a phenolic steroid adenosine 3',5'-bisphosphate + steroid O-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and phenolic steroid, whereas its two products are adenosine 3',5'-bisphosphate and steroid O-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:phenolic-steroid sulfotransferase. This enzyme is also called steroid alcohol sulfotransferase. This enzyme participates in steroid metabolism.
Genes
Of 62 sulfotransferase genes in the human genome, 16 represent cytoplasmic sulfotransferases, and of these 16 cytoplasmic sulfotransferases, five have been found to act as steroid sulfotransferases. These five sulfotransferase genes are SULT1A1, SULT1E1, and SULT2A1, as well as the two isoforms of SULT2B1, SULT2B1a and SULT2B1b. Their substrate specificity is as follows:
SULT1A1: Estradiol (to estradiol sulfate)
SULT1E1: (to sulfate); Estrone (to estrone sulfate); Estradiol (to estradiol sulfate)
SULT2A1: (to sulfate); Androsterone (to androsterone sulfate); Pregnenolone (to pregnenolone sulfate)
SULT2B1a: Pregnenolone (to pregnenolone sulfate)
SULT2B1b: Cholesterol (to cholesterol sulfate)
Traditionally, steroid sulfotransferases have been named according |
https://en.wikipedia.org/wiki/Succinate%E2%80%94citramalate%20CoA-transferase | In enzymology, a succinate-citramalate CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + citramalate succinate + citramalyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and citramalate, whereas its two products are succinate and citramalyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:citramalate CoA-transferase. Other names in common use include itaconate CoA-transferase, citramalate CoA-transferase, citramalate coenzyme A-transferase, and succinyl coenzyme A-citramalyl coenzyme A transferase. This enzyme participates in c5-branched dibasic acid metabolism.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinate%E2%80%94hydroxymethylglutarate%20CoA-transferase | In enzymology, a succinate-hydroxymethylglutarate CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + 3-hydroxy-3-methylglutarate succinate + (S)-3-hydroxy-3-methylglutaryl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and 3-hydroxy-3-methylglutarate, whereas its two products are succinate and (S)-3-hydroxy-3-methylglutaryl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase. Other names in common use include hydroxymethylglutarate coenzyme A-transferase, and dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinyl-CoA%3A%28R%29-benzylsuccinate%20CoA-transferase | In enzymology, a succinyl-CoA:(R)-benzylsuccinate CoA-transferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + (R)-2-benzylsuccinate succinate + (R)-2-benzylsuccinyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and (R)-2-benzylsuccinate, whereas its two products are succinate and (R)-2-benzylsuccinyl-CoA.
This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is succinyl-CoA:(R)-2-benzylsuccinate CoA-transferase. This enzyme is also called benzylsuccinate CoA-transferase. This enzyme participates in benzoate degradation via coa ligation.
References
EC 2.8.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiol%20sulfotransferase | In enzymology, a thiol sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + a thiol adenosine 3',5'-bisphosphate + an S-alkyl thiosulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and thiol, whereas its two products are adenosine 3',5'-bisphosphate and S-alkyl thiosulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:thiol S-sulfotransferase. Other names in common use include phosphoadenylylsulfate-thiol sulfotransferase, PAPS sulfotransferase, and adenosine 3'-phosphate 5'-sulphatophosphate sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiosulfate%E2%80%94dithiol%20sulfurtransferase | In enzymology, a thiosulfate-dithiol sulfurtransferase () is an enzyme that catalyzes the chemical reaction
thiosulfate + dithioerythritol sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized dithioerythritol) + sulfide
Thus, the two substrates of this enzyme are thiosulfate and dithioerythritol, whereas its 3 products are sulfite, 4,5-cis-dihydroxy-1,2-dithiacyclohexane, and sulfide.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:dithioerythritol sulfurtransferase. Other names in common use include thiosulfate reductase, and TSR. This enzyme participates in sulfur metabolism.
References
EC 2.8.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiosulfate%E2%80%94thiol%20sulfurtransferase | In enzymology, a thiosulfate-thiol sulfurtransferase () is an enzyme that catalyzes the chemical reaction
thiosulfate + 2 glutathione sulfite + glutathione disulfide + sulfide
Thus, the two substrates of this enzyme are thiosulfate and glutathione, whereas its 3 products are sulfite, glutathione disulfide, and sulfide.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:thiol sulfurtransferase. Other names in common use include glutathione-dependent thiosulfate reductase, sulfane reductase, and sulfane sulfurtransferase. This enzyme participates in glutathione metabolism.
References
EC 2.8.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Triglucosylalkylacylglycerol%20sulfotransferase | In enzymology, a triglucosylalkylacylglycerol sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + α-D-glucosyl-(1→6)-alpha-D-glucosyl-(1→6)-α-D-glucosyl-(1→3)-1-O-alkyl-2-O-acylglycerol adenosine 3',5'-bisphosphate + 6-sulfo-α-D-glucosyl-(1→6)-α-D-glucosyl-(1→6)-α-D-glucosyl-(1→3)-1-O-alkyl-2-O-acylglycerol
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:triglucosyl-1-O-alkyl-2-O-acylglycerol 6-sulfotransferase. This enzyme is also called triglucosylmonoalkylmonoacyl sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/TRNA%20sulfurtransferase | In enzymology, a tRNA sulfurtransferase () is an enzyme that catalyzes the chemical reaction
L-cysteine + 'activated' tRNA L-serine + tRNA containing a thionucleotide
Thus, the two substrates of this enzyme are L-cysteine and 'activated' tRNA, whereas its two products are L-serine and tRNA containing a thionucleotide.
This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:tRNA sulfurtransferase. Other names in common use include transfer ribonucleate sulfurtransferase, RNA sulfurtransferase, ribonucleate sulfurtransferase, transfer RNA sulfurtransferase, and transfer RNA thiolase.
References
EC 2.8.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Tyrosine-ester%20sulfotransferase | In enzymology, a tyrosine-ester sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + L-tyrosine methyl ester adenosine 3',5'-bisphosphate + L-tyrosine methyl ester 4-sulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and L-tyrosine methyl ester, whereas its two products are adenosine 3',5'-bisphosphate and L-tyrosine methyl ester 4-sulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:L-tyrosine-methyl-ester sulfotransferase. Other names in common use include aryl sulfotransferase IV, and L-tyrosine methyl ester sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/UDP-N-acetylgalactosamine-4-sulfate%20sulfotransferase | In enzymology, an UDP-N-acetylgalactosamine-4-sulfate sulfotransferase () is an enzyme that catalyzes the chemical reaction
3'-phosphoadenylyl sulfate + UDP-N-acetyl-D-galactosamine 4-sulfate adenosine 3',5'-bisphosphate + UDP-N-acetyl-D-galactosamine 4,6-bissulfate
Thus, the two substrates of this enzyme are 3'-phosphoadenylyl sulfate and UDP-N-acetyl-D-galactosamine 4-sulfate, whereas its two products are adenosine 3',5'-bisphosphate and UDP-N-acetyl-D-galactosamine 4,6-bissulfate.
This enzyme belongs to the family of transferases, specifically the sulfotransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is 3'-phosphoadenylyl-sulfate:UDP-N-acetyl-D-galactosamine-4-sulfate 6-sulfotransferase. Other names in common use include uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase, uridine diphospho-N-acetylgalactosamine 4-sulfate sulfotransferase, and uridine diphosphoacetylgalactosamine 4-sulfate sulfotransferase.
References
EC 2.8.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/CLRN1 | Clarin-1 is a protein that in humans is encoded by the CLRN1 gene.
Function
This gene encodes a protein that contains a cytosolic N-terminus, multiple helical transmembrane domains, and an endoplasmic reticulum membrane retention signal, TKGH, in the C-terminus. The encoded protein may be important in development and homeostasis of the inner ear and retina. Mutations within this gene have been associated with Usher syndrome type IIIa. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Retinitis Pigmentosa Overview |
https://en.wikipedia.org/wiki/Sodium%20bicarbonate%20cotransporter%203 | Sodium bicarbonate cotransporter 3 is a protein which in humans is encoded by the SLC4A7 gene.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/USH1C | Harmonin is a protein that in humans is encoded by the USH1C gene. It is expressed in sensory cells of the inner ear and retina, where it plays a role in hearing, balance, and vision. Mutations at the USH1C locus cause Usher syndrome type 1c and nonsyndromic sensorineural deafness.
Gene and protein structure
The USH1C gene is located on chromosome 11 and contains 28 exons. Alternative splicing generates multiple mRNA transcript variants, some of which are associated with the rare disorder phenotypes of Usher syndrome and nonsyndromic sensorineural deafness. The encoded protein harmonin has multiple protein isoforms due to the alternative splicing, including a standard isoform with 552 amino acids. Harmonin contains a PDZ domain, which assists in attaching the protein to the cell membrane and to cytoskeletal components.
Inner ear function
Harmonin is found at the apex of inner hair cells (IHCs), which convert mechanical signals from sound waves into electrical signals interpreted by the brain as sound. IHCs have an apical bundle of actin-rich stereocilia that vary in height and are connected to each other by flexible tip links. Tip links are protein complexes of cadherin 23 (CDH23) and protocadherin 15 (PCDH15). Harmonin binds to proteins that are involved in connecting the tip link to the cytoskeleton. Sound waves physically displace the bundle towards the tallest stereocilium, stretching the tip links and causing mechanically gated ion channels to open. Influx of calci |
https://en.wikipedia.org/wiki/CDH23 | Cadherin-23 is a protein that in humans is encoded by the CDH23 gene.
Function
This gene is a member of the cadherin superfamily, genes encoding calcium dependent cell-cell adhesion glycoproteins. The protein encoded by this gene is a large, single-pass transmembrane protein composed of an extracellular domain containing 27 repeats that show significant homology to the cadherin ectodomain. Expressed in the neurosensory epithelium, the protein is thought to be involved in stereocilia organization and hair bundle formation. Specifically, it is thought to interact with protocadherin 15 to form tip-link filaments.
Clinical significance
The gene is located in a region containing the human deafness loci DFNB12 and USH1D. Usher syndrome 1D and nonsyndromic autosomal recessive deafness DFNB12 are caused by allelic mutations of this novel cadherin-like gene. The gene is associated with kidney function decline.
Interactions
CDH23 has been shown to interact with USH1C.
References
Further reading
External links |
https://en.wikipedia.org/wiki/PCDH15 | Protocadherin-15 is a protein that in humans is encoded by the PCDH15 gene.
Function
This gene is a member of the cadherin superfamily. Family members encode integral membrane proteins that mediate calcium-dependent cell-cell adhesion. The protein product of this gene consists of a signal peptide, 11 extracellular calcium-binding domains, a transmembrane domain and a unique cytoplasmic domain. It plays an essential role in maintenance of normal retinal and cochlear function. It is thought to interact with CDH23 to form tip-link filaments.
Clinical significance
Mutations in this gene have been associated with hearing loss, which is consistent with its location at the Usher syndrome type 1F (USH1F) critical region on chromosome 10. Variation within it has also been found to be associated with normal differences in human facial appearance.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Usher Syndrome Type I
PDBe-KB provides an overview of all the structure information available in the PDB for Human Protocadherin-15 (PCDH15) |
https://en.wikipedia.org/wiki/GPR98 | ADGRV1, also known as G protein-coupled receptor 98 (GPR98) or Very Large G-protein coupled receptor 1 (VLGR1), is a protein that in humans is encoded by the GPR98 gene. Several alternatively spliced transcripts have been described.
The adhesion GPCR VLGR1 is the largest GPCR known, with a size of 6300 amino acids and consisting of 90 exons. There are 8 splice variants of VlgR1, named VlgR1a-1e and Mass1.1-1.3. The N-terminus consists of 5800 amino acids containing 35 Calx-beta domains, one pentraxin domain, and one epilepsy associated repeat. Mutations of VlgR1 have been shown to result in Usher's syndrome. Knockouts of Vlgr1 in mice have been shown to phenocopy Usher's syndrome and lead to audiogenic seizures.
Function
This gene encodes a member of the adhesion-GPCR family of receptors. The protein binds calcium and is expressed in the central nervous system. It is also known as very large G-protein coupled receptor 1 because it is 6300 residues long. It contains a C-terminal 7-transmembrane receptor domain, whereas the large N-terminal segment (5900 residues) includes 35 calcium binding Calx-beta domains, and 6 EAR domains.
Evolution
The sea urchin genome has a homolog of VLGR1 in it.
Clinical significance
Mutations in this gene are associated with Usher syndrome 2 and familial febrile seizures.
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Usher Syndrome Type II
Receptors
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Vogt%E2%80%93Russell%20theorem | The Vogt–Russell theorem states that the structure of a star, in hydrostatic and thermal equilibrium with all energy derived from nuclear reactions, is uniquely determined by its mass and the distribution of chemical elements throughout its interior. Although referred to as a theorem, the Vogt–Russell theorem has never been formally proved. The theorem is named after astronomers Heinrich Vogt and Henry Norris Russell, who devised it independently.
References
Stellar astronomy |
https://en.wikipedia.org/wiki/Asfarviridae | Asfarviridae is a family of viruses, the best-studied of which is African swine fever virus, which are double-stranded DNA viruses.
Taxonomy
There is only one species under Asfarviridae in ICTV 2022:
Genus Asfivirus
Species African swine fever virus
But, there may be more viruses:
Abalone asfarvirus
Dinodnavirus (Heterocapsa circularisquama DNA virus or hcDNAV)
Faustovirus
Kaumoebavirus
Pacmanvirus
Additional genomes known from environmental sampling of diverse marine, freshwater, and terrestrial habitats
References
Nucleocytoplasmic large DNA viruses
Virus families |
https://en.wikipedia.org/wiki/Deltaarterivirus%20hemfev | Deltaarterivirus hemfev, formerly Simian hemorrhagic fever virus or simian haemorrhagic fever virus (SHFV), is a highly pathogenic virus in monkeys. It is a positive-stranded RNA virus classified in the family Arteriviridae. It is the only member of the subgenus Hedartevirus.
Hosts
Patas are believed to be the natural host for the virus since about 50% of wild patas monkeys have antibodies for the virus, while antibodies are much less prevalent in other simian species such as vervets and baboons. In macaques, however, infection with this virus can result in acute severe disease with high mortality. Recently, red colobus monkeys and red-tailed guenons have been identified as natural hosts for SHFV.
In 2022, scientists cautioned about potential future spillover of SHFV.
Symptoms
Asymptomatic infection of the virus can occur in patas monkeys, vervet monkeys, and baboons, although it is observed primarily in patas monkeys. Infection has a rapid onset with animals developing a high fever, facial edema, cyanosis, anorexia, melena, and may begin to hemorrhage at the cutaneous, subcutaneous, and retrobulbar levels. Thrombocytopenia will develop soon after. Death usually occurs within 10–15 days after symptoms appear.
References
Arteriviridae
Hemorrhagic fevers |
https://en.wikipedia.org/wiki/Bronze%20%28disambiguation%29 | Bronze is an alloy of copper with any of several other metals, often tin.
Bronze may also refer to:
Bronze (color), the tint of the metal
Bronze (horse), a racehorse
Bronze (racial classification), persons of combined Latin European and Indigenous American ancestry
Bronze (turkey), a breed of domestic turkey
Bronze Age, an early period of historical development
Bronze Night, a series of riots in Estonia in 2007
Bronze Records, an English independent record label
Bronze sculpture, a piece of art made of bronze
Bronze Soldier of Tallinn, a controversial Soviet WW2 Monument in Tallinn, Estonia
Bronze Sunbird, a species of bird found in Africa
In chemistry, various mixed oxides with metallic sheen, such as
Sodium tungsten bronze
Molybdenum purple bronze , A = Li, Na, K, Rb, Tl
Lucy Bronze (born 1991), English association footballer
The Bronze (film), a 2015 comedy film
The Bronze, a fictional nightclub in Buffy the Vampire Slayer
See also
Bronze Cross (disambiguation)
Bronze Medal (disambiguation)
Bronze Medallion (disambiguation), an award in several organizations
Bronze star (disambiguation)
Bronz, a musical group
Bronzer, a tanning product
Bronzing, a process by which an object is preserved by electroplating with copper
Compact disc bronzing |
https://en.wikipedia.org/wiki/Varicosavirus | Varicosavirus is a genus of plant viruses. The virus is associated with swelling in plant vein tissues. They are negative single stranded RNA viruses. The genus contains three species.
Taxonomy
The genus contains the following species:
Alopecurus varicosavirus
Lettuce big-vein associated varicosavirus
Trifolium varicosavirus
Structure
Virions consist of a non-enveloped rod-shaped capsid, having a helical symmetry of 120–360 nm in length, and a width of 18–30 nm.
Genome
The genome consists of a bi-segmented linear, single-stranded negative sense RNA. The first segment is about 6350–7000 nucleotides in length; the second, about 5630–6500 nucleotides in length.
References
External links
Viralzone: Varicosavirus
Varicosaviruses
Virus genera |
https://en.wikipedia.org/wiki/Bulk%20temperature | In thermofluids dynamics, the bulk temperature, or the average bulk temperature in the thermal fluid, is a convenient reference point for evaluating properties related to convective heat transfer, particularly in applications related to flow in pipes and ducts.
The concept of the bulk temperature is that adiabatic mixing of the fluid from a given cross section of the duct will result in some equilibrium temperature that accurately reflects the average temperature of the moving fluid, more so than a simple average like the film temperature.
References
Continuum mechanics
Heat transfer
Temperature |
https://en.wikipedia.org/wiki/G%20alpha%20subunit | G alpha subunits are one of the three types of subunit of guanine nucleotide binding proteins, which are membrane-associated, heterotrimeric G proteins.
Background
G proteins and their receptors (GPCRs) form one of the most prevalent signaling systems in mammalian cells, regulating systems as diverse as sensory perception, cell growth and hormonal regulation. At the cell surface, the binding of ligands such as hormones and neurotransmitters to a GPCR activates the receptor by causing a conformational change, which in turn activates the bound G protein on the intracellular-side of the membrane. The activated receptor promotes the exchange of bound GDP for GTP on the G protein alpha subunit. GTP binding changes the conformation of switch regions within the alpha subunit, which allows the bound trimeric G protein (inactive) to be released from the receptor, and to dissociate into active alpha subunit (GTP-bound) and beta/gamma dimer. The alpha subunit and the beta/gamma dimer go on to activate distinct downstream effectors, such as adenylyl cyclase, phosphodiesterases, phospholipase C, and ion channels. These effectors in turn regulate the intracellular concentrations of secondary messengers, such as cAMP, diacylglycerol, sodium or calcium cations, which ultimately lead to a physiological response, usually via the downstream regulation of gene transcription. The cycle is completed by the hydrolysis of alpha subunit-bound GTP to GDP, resulting in the re-association of the alpha |
https://en.wikipedia.org/wiki/KMT2A | Histone-lysine N-methyltransferase 2A, also known as acute lymphoblastic leukemia 1 (ALL-1), myeloid/lymphoid or mixed-lineage leukemia 1 (MLL1), or zinc finger protein HRX (HRX), is an enzyme that in humans is encoded by the KMT2A gene.
MLL1 is a histone methyltransferase deemed a positive global regulator of gene transcription. This protein belongs to the group of histone-modifying enzymes comprising transactivation domain 9aaTAD and is involved in the epigenetic maintenance of transcriptional memory. Its role as an epigenetic regulator of neuronal function is an ongoing area of research.
Function
Transcriptional regulation
KMT2A gene encodes a transcriptional coactivator that plays an essential role in regulating gene expression during early development and hematopoiesis. The encoded protein contains multiple conserved functional domains. One of these domains, the SET domain, is responsible for its histone H3 lysine 4 (H3K4) methyltransferase activity which mediates chromatin modifications associated with epigenetic transcriptional activation. Enriched in the nucleus, the MLL1 enzyme trimethylates H3K4 (H3K4me3). It also upregulates mono- and dimethylation of H3K4. This protein is processed by the enzyme Taspase 1 into two fragments, MLL-C (~180 kDa) and MLL-N (~320 kDa). These fragments then assemble into different multi-protein complexes that regulate the transcription of specific target genes, including many of the HOX genes.
Transcriptome profiling after deletion |
https://en.wikipedia.org/wiki/Saint-Venant%27s%20theorem | In solid mechanics, it is common to analyze the properties of beams with constant cross section. Saint-Venant's theorem states that the simply connected cross section with maximal torsional rigidity is a circle. It is named after the French mathematician Adhémar Jean Claude Barré de Saint-Venant.
Given a simply connected domain D in the plane with area A, the radius and the area of its greatest inscribed circle, the torsional rigidity P
of D is defined by
Here the supremum is taken over all the continuously differentiable functions vanishing on the boundary of D. The existence of this supremum is a consequence of Poincaré inequality.
Saint-Venant conjectured in 1856 that
of all domains D of equal area A the circular one has the greatest torsional rigidity, that is
A rigorous proof of this inequality was not given until 1948 by Pólya. Another proof was given by Davenport and reported in. A more general proof and an estimate
is given by Makai.
Notes
Elasticity (physics)
Eponymous theorems of physics
Calculus of variations
Inequalities |
https://en.wikipedia.org/wiki/Comeau%20C/C%2B%2B | Comeau C/C++ is a compiler for C and C++ produced by Comeau Computing. Comeau C/C++ was once described as the most standards-conformant C++ compiler. In 2006-2008 it was described as the only mainstream C++ compiler to fully support the export keyword for exported templates.
Design
The compiler supports several dialects of both the C and C++ languages. It comes with its own version of the Standard C++ library, libcomo, that is based upon the Standard C++ library from Silicon Graphics, but can also be used with the Dinkumware Standard C library.
The compiler is based upon the Edison Design Group C++ frontend, also utilized in the Intel C++ Compiler. Rather than produce an executable directly, Comeau C/C++ outputs C code and requires a separate C compiler in order to produce the final program. The Comeau C/C++ can employ several back ends.
Standards compliance
Comeau Computing is a founding member of the C++ committee. Comeau Computing's CEO, Greg Comeau, provided one of the early ports of cfront to the PC.
Distribution
A limited-function version of the compiler, which allows one to compile source code and view any resulting error messages, but not to produce executable programs, is available from the company's web site.
The compiler is available for both Unix and Microsoft Windows platforms. Comeau also offers custom ports to other platforms, albeit that this is substantially more expensive than buying existent versions of the compiler.
Status
The compiler was upd |
https://en.wikipedia.org/wiki/Sonotone%201010 | The Sonotone 1010 hearing aid was introduced on 29 December 1952. It was the first commercial product to use transistors, which had been invented five years earlier in 1947.
It was a hybrid design, using two miniature vacuum tubes as input stages and a single transistor as the output stage; this was required because the transistors at the time produced too much electrical noise. Even using one transistor considerably extended battery life, lowering the operating cost of the unit. As transistors improved, this model was replaced by all-transistor hearing aids.
The Sonotone company had its headquarters in New York City and was established in 1929. The company was bought by various other companies and was no longer in business by 2005.
See also
Deafness
History of hearing aids
References
Hearing aids |
https://en.wikipedia.org/wiki/Stribeck%20curve | The Stribeck curve is a fundamental concept in the field of tribology. It shows that friction in fluid-lubricated contacts is a non-linear function of the contact load, the lubricant viscosity and the lubricant entrainment speed. The discovery and underlying research is usually attributed to Richard Stribeck and Mayo D. Hersey, who studied friction in journal bearings for railway wagon applications during the first half of the 20th century; however, other researchers have arrived at similar conclusions before. The mechanisms along the Stribeck curve have been understood today also on the atomistic level.
Concept
For a contact of two fluid-lubricated surfaces, the Stribeck curve shows the relationship between the so-called Hersey number, a dimensionless lubrication parameter, and the friction coefficient. The Hersey number is defined as:
where η is the dynamic viscosity of the fluid, N is the entrainment speed of the fluid and P is the normal load per length of the tribological contact.
Hersey's original formula uses the rotational speed (revolutions per unit time) for N and the load per projected area (i.e. the product of a journal bearing's length and diameter) for P.
Alternatively, the Hersey number is the dimensionless number obtained from the velocity (m/s) times the dynamic viscosity (Pa∙s = N∙s/m2), divided by the load per unit length of bearing (N/m).
Thus, for a given viscosity and load, the Stribeck curve shows how friction changes with increasing velocity. |
https://en.wikipedia.org/wiki/Marnaviridae | Marnaviridae is a family of positive-stranded RNA viruses in the order Picornavirales that infect various photosynthetic marine protists. Members of the family have non-enveloped, icosahedral capsids. Replication occurs in the cytoplasm and causes lysis of the host cell. The first species of this family that was isolated is Heterosigma akashiwo RNA virus (HaRNAV) in the genus Marnavirus, which infects the toxic bloom-forming Raphidophyte alga, Heterosigma akashiwo. As of 2021, there are twenty species across seven genera in this family, as well as many other related virus sequences discovered through metagenomic sequencing that are currently unclassified.
Interactions between members of the Marnaviridae family and their hosts have notable significance in marine ecology, and are also relevant within the aquaculture industry. HaRNAV and viruses from Bacillarnavirus are known to have roles in regulating dynamics and composition of their hosts’ blooms. An unclassified sequence, Baishivirus, has been suggested to be the possible pathogen of glass post-larvae disease, which is prevalent in shrimp aquaculture. Viruses detected in a cultured prawn species that had been affected by growth retardation disease have also been placed in Marnaviridae.
History
The name "marnaviridae" is based on its genome type (RNA virus - rnaviridae), together with the prefix "ma" being derived from the Latin word mare (sea).
The family was proposed following the discovery of an RNA virus (HaRNAV) tha |
https://en.wikipedia.org/wiki/Crystal%20Lake%20Falls%20Historic%20District | The Crystal Lake Falls Historic District, also known as the Brick Kingdom, is a historic industrial and residential area in Barton, Vermont, United States. It is located along Water Street and Main Street, roughly paralleling Willoughby Brook, whose waters powered the area's industries. It was added to the U.S. National Register of Historic Places on August 7, 1994.
The Brick Kingdom
The Crystal Lake Falls Historic District covers several blocks of Barton village, located at northwest corner of Crystal Lake. It extends roughly along Water Street from Church to Main Street, along Main from Water to Duck Pond Road, and along West Street from Cemetery Road to Main Street. The latter areas is known colloquially as the "Brick Kingdom", and runs roughly parallel to Willoughby Brook, the outflow from Crystal Lake, which drops about in a series of falls. The earliest documented industrial activity on the falls began in the 1790s, with Asa Kimball starting a sawmill in 1798 and a gristmill in 1807 on the upper falls. During the 19th century, factories clustered along Water Street, with a variety of manufacturing activities. Businesses located here manufactured piano works, furniture, ladies cotton lingerie and baseball bats. These mostly closed by the 1940s, with the last leaving in 1952. The mills employed about 300 workers.
Mills and other local industrial activities included the following:
Heyward Chair Company 1860–1890
Charles Ufford Carriage Maker 1868 – circa 1892
Bar |
https://en.wikipedia.org/wiki/Microsoft%20Phoenix | Microsoft Phoenix was an SDK available from Microsoft Connect for creating compilers, optimize code, and perform code analysis. Microsoft described it in the past tense on 2008-07-01.
Original Description
[It was] to be used as the back-end for future compiler technologies from Microsoft. It [was] also available as an SDK, a pre-release build of which has been made accessible, to create compilers and code analysis tools using the Phoenix framework.
Overview
Microsoft Phoenix defines an intermediate representation (IR) for programs, using ASTs, control-flow graphs, and an exception handling model. For any program to be handled by Phoenix, it needs to be converted to this representation. The specification for these file type-specific converters, called file readers in Phoenix terminology, is also specified. Phoenix comes included with readers for Portable Executable binary files, CIL and the output of the Visual C++ front-end. Readers for other languages can be written using the Phoenix SDK, though separate tools such as lex and yacc need to be used to write the lexer and parser, respectively.
Once the program has been converted to the IR, the analysis and optimization tools can operate on that form. Phoenix includes a selection of tools – including block counting, memory analysis, code coverage, code analysis and optimization. The Phoenix SDK can be used to write and plug-in other tools as well. Code generation is handled by providing architecture-specific (either physical |
https://en.wikipedia.org/wiki/Jeff%20Gill%20%28academic%29 | Jefferson Morris Gill (born December 22, 1960) is Distinguished Professor of Government, and of Mathematics & Statistics, the Director of the Center for Data Science, the Editor of Political Analysis, and a member of the Center for Behavioral Neuroscience at American University as of the Fall of 2017.
He was a Professor of Political Science at Washington University in St. Louis and the Director of the Center for Applied Statistics. He was also President of the Society for Political Methodology, and is an inaugural fellow of the Society for Political Methodology. Major areas of research and interest include: Political Methodology, American Politics, Statistical Computing, Research Methods, and Public Administration. Current research is focused on projects on work in the development of Bayesian hierarchical models, nonparametric Bayesian models, elicited prior development from expert interviews, as well in fundamental issues in statistical inference. He has extensive expertise in statistical computing, Markov chain Monte Carlo (MCMC) tools in particular. Most sophisticated Bayesian models for the social or medical sciences require complex, compute-intensive tools such as MCMC to efficiently estimate parameters of interest. Gill is an expert in these statistical and computational techniques and uses them to contribute to empirical knowledge in the biomedical and social sciences. Current theoretical work builds logically on Gill's prior applied work and adds opportunities t |
https://en.wikipedia.org/wiki/2%2C6-dioxo-6-phenylhexa-3-enoate%20hydrolase | In enzymology, a 2,6-dioxo-6-phenylhexa-3-enoate hydrolase () is an enzyme that catalyzes the chemical reaction
2,6-dioxo-6-phenylhexa-3-enoate + H2O benzoate + 2-oxopent-4-enoate
Thus, the two substrates of this enzyme are 2,6-dioxo-6-phenylhexa-3-enoate and H2O, whereas its two products are benzoate and 2-oxopent-4-enoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase. This enzyme is also called HOHPDA hydrolase. This enzyme participates in biphenyl degradation and fluorene degradation.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2%27-hydroxybiphenyl-2-sulfinate%20desulfinase | In enzymology, a 2'-hydroxybiphenyl-2-sulfinate desulfinase () is an enzyme that catalyzes the chemical reaction
2'-hydroxybiphenyl-2-sulfinate + H2O 2-hydroxybiphenyl + sulfite
Thus, the two substrates of this enzyme are 2'-hydroxybiphenyl-2-sulfinate and H2O, whereas its two products are 2-hydroxybiphenyl and sulfite.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-sulfur bonds. The systematic name of this enzyme class is 2'-hydroxybiphenyl-2-sulfinate sulfohydrolase. Other names in common use include gene dszB-encoded hydrolase, 2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase, DszB, HBPSi desulfinase, 2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase, HPBS desulfinase, 2-(2-hydroxyphenyl)benzenesulfinate hydrolase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase, and 2-(2-hydroxyphenyl)benzenesulfinate desulfinase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.13.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2-hydroxymuconate-semialdehyde%20hydrolase | In enzymology, a 2-hydroxymuconate-semialdehyde hydrolase () is an enzyme that catalyzes the chemical reaction
2-hydroxymuconate semialdehyde + H2O formate + 2-oxopent-4-enoate
Thus, the two substrates of this enzyme are 2-hydroxymuconate semialdehyde and H2O, whereas its two products are formate and 2-oxopent-4-enoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2-hydroxymuconate-semialdehyde formylhydrolase. Other names in common use include 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase, 2-hydroxymuconic semialdehyde hydrolase, HMSH, and HOD hydrolase. This enzyme participates in 5 metabolic pathways: benzoate degradation via hydroxylation, toluene and xylene degradation, 1,4-dichlorobenzene degradation, carbazole degradation, and styrene degradation.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and .
References
EC 3.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-chlorobenzoate%20dehalogenase | In enzymology, a 4-chlorobenzoate dehalogenase () is an enzyme that catalyzes the chemical reaction
4-chlorobenzoate + H2O 4-hydroxybenzoate + chloride
Thus, the two substrates of this enzyme are 4-chlorobenzoate and H2O, whereas its two products are 4-hydroxybenzoate and chloride.
This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is 4-chlorobenzoate chlorohydrolase. This enzyme is also called halobenzoate dehalogenase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.8.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/4-chlorobenzoyl-CoA%20dehalogenase | In enzymology, a 4-chlorobenzoyl-CoA dehalogenase () is an enzyme that catalyzes the chemical reaction
4-chlorobenzoyl-CoA + H2O 4-hydroxybenzoyl CoA + chloride
Thus, the two substrates of this enzyme are 4-chlorobenzoyl-CoA and H2O, whereas its two products are 4-hydroxybenzoyl CoA and chloride.
This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is 4-chlorobenzoyl CoA chlorohydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.
References
EC 3.8.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acetylpyruvate%20hydrolase | In enzymology, an acetylpyruvate hydrolase () is an enzyme that catalyzes the chemical reaction
acetylpyruvate + H2O acetate + pyruvate
Thus, the two substrates of this enzyme are acetylpyruvate and H2O, whereas its two products are acetate and pyruvate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2,4-dioxopentanoate acetylhydrolase.
References
EC 3.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acylpyruvate%20hydrolase | In enzymology, an acylpyruvate hydrolase () is an enzyme that catalyzes the chemical reaction
a 3-acylpyruvate + H2O a carboxylate + pyruvate
Thus, the two substrates of this enzyme are 3-acylpyruvate and water, whereas its two products are carboxylate and pyruvate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 3-acylpyruvate acylhydrolase. This enzyme participates in tyrosine metabolism.
References
EC 3.7.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Prehypertension | Prehypertension, also known as high normal blood pressure and borderline hypertensive (BH), is a medical classification for cases where a person's blood pressure is elevated above optimal or normal, but not to the level considered hypertension (high blood pressure). Prehypertension is now referred to as "elevated blood pressure" by the American College of Cardiology (ACC) and the American Heart Association (AHA). The ACC/AHA define elevated blood pressure as readings with a systolic pressure from 120 to 129 mm Hg and a diastolic pressure under 80 mm Hg, and the European Society of Cardiology and European Society of Hypertension (ESC/ESH) define "high normal blood pressure" as readings with a systolic pressure from 130 to 139 mm Hg and a diastolic pressure 85-89 mm Hg. Readings greater than or equal to 130/80 mm Hg are considered hypertension by ACC/AHA and if greater than or equal to 140/90 mm Hg by ESC/ESH.
Classification of blood pressure is based upon two or more readings at two or more separate occasions, and compared to out-of-office blood pressure readings if possible.
Signs and symptoms
Prehypertension is often asymptomatic (without symptoms) at the time of diagnosis. Only extremely elevated blood pressure (malignant hypertension) can, in rare cases, cause headaches, visual changes, fatigue, or dizziness, but these are nonspecific symptoms which can occur with many other conditions. Thus, blood pressures above normal can go undiagnosed for a long period of time.
|
https://en.wikipedia.org/wiki/Alkylhalidase | In enzymology, an alkylhalidase () is an enzyme that catalyzes the chemical reaction
bromochloromethane + H2O formaldehyde + bromide + chloride
Thus, the two substrates of this enzyme are bromochloromethane and H2O, whereas its 3 products are formaldehyde, bromide, and chloride.
This enzyme belongs to the family of hydrolases, specifically those acting on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is alkyl-halide halidohydrolase. Other names in common use include halogenase, haloalkane halidohydrolase, and haloalkane dehalogenase.
References
Further reading
EC 3.8.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-diketone%20hydrolase | In enzymology, a beta-diketone hydrolase () is an enzyme that catalyzes the chemical reaction
nonane-4,6-dione + H2O pentan-2-one + butanoate
Thus, the two substrates of this enzyme are nonane-4,6-dione and H2O, whereas its two products are 2-pentanone and butanoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is nonane-4,6-dione acylhydrolase. This enzyme is also called oxidized PVA hydrolase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.7.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cyclamate%20sulfohydrolase | In enzymology, a cyclamate sulfohydrolase () is an enzyme that catalyzes the chemical reaction
cyclohexylsulfamate + H2O cyclohexylamine + sulfate
Thus, the two substrates of this enzyme are cyclohexylsulfamate and H2O, whereas its two products are cyclohexylamine and sulfate.
This enzyme belongs to the family of hydrolases, specifically those acting on sulfur-nitrogen bonds. The systematic name of this enzyme class is cyclohexylsulfamate sulfohydrolase. Other names in common use include cyclamate sulfamatase, cyclamate sulfamidase, and cyclohexylsulfamate sulfamidase. This enzyme participates in caprolactam degradation.
References
EC 3.10.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyclohexane-1%2C3-dione%20hydrolase | In enzymology, a cyclohexane-1,3-dione hydrolase () is an enzyme that catalyzes the chemical reaction
cyclohexane-1,3-dione + H2O 5-oxohexanoate
Thus, the two substrates of this enzyme are cyclohexane-1,3-dione and H2O, whereas its product is 5-oxohexanoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is cyclohexane-1,3-dione acylhydrolase (decyclizing). This enzyme is also called 1,3-cyclohexanedione hydrolase.
References
EC 3.7.1
Enzymes of unknown structure |
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