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https://en.wikipedia.org/wiki/S-adenosylhomocysteine%20deaminase | In enzymology, a S-adenosylhomocysteine deaminase () is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-homocysteine + H2O S-inosyl-L-homocysteine + NH3
Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.
References
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Sepiapterin%20deaminase | In enzymology, a sepiapterin deaminase () is an enzyme that catalyzes the chemical reaction
sepiapterin + H2O xanthopterin-B2 + NH3
Thus, the two substrates of this enzyme are sepiapterin and H2O whereas its two products are xanthopterin-B2 and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is sepiapterin aminohydrolase.
References
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/%28S%29-N-acetyl-1-phenylethylamine%20hydrolase | In enzymology, a (S)-N-acetyl-1-phenylethylamine hydrolase () is an enzyme that catalyzes the chemical reaction
N-acetylphenylethylamine + HO phenethylamine + acetate
Thus, the two substrates of this enzyme are N-acetylphenylethylamine and HO, whereas its two products are phenethylamine and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (S)-N-acetylphenylethylamine:HO hydrolase. At least one compound, phenylmethanesulfonylfluoride is known to inhibit this enzyme.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Succinyl-diaminopimelate%20desuccinylase | In enzymology, a succinyl-diaminopimelate desuccinylase () is an enzyme that catalyzes the chemical reaction
N-succinyl-LL-2,6-diaminoheptanedioate + H2O succinate + LL-2,6-diaminoheptanedioate
Thus, the two substrates of this enzyme are N-succinyl-LL-2,6-diaminoheptanedioate and H2O, whereas its two products are succinate and LL-2,6-diaminoheptanedioate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is . This enzyme is also called . This enzyme participates in lysine biosynthesis.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Paul%20W.%20Chun | Paul W. Chun is a professor emeritus at the University of Florida. He is a researcher in the field of protein folding equilibria, in particular, he is known as the "leading proponent" of using the Planck-Benzinger thermal work function to understand protein folding thermodynamics and stability. As such Chun has written a number of papers relating to the thermodynamics of protein folding. He received his Ph.D. in 1965 from the University of Missouri for work on the interaction of casein molecules, and joined the department of biochemistry and molecular biology at the University of Florida soon thereafter. He retired in 2003.
He has published 68 peer-reviewed papers listed in Scopus.
References
External links
Home page.
Year of birth missing (living people)
Living people
University of Florida faculty
University of Missouri alumni
American biochemists
American molecular biologists
Thermodynamicists |
https://en.wikipedia.org/wiki/Succinylglutamate%20desuccinylase | In enzymology, a succinylglutamate desuccinylase () is an enzyme that catalyzes the chemical reaction
N-succinyl-L-glutamate + H2O succinate + L-glutamate
Thus, the two substrates of this enzyme are N-succinyl-L-glutamate and H2O, whereas its two products are succinate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-succinyl-L-glutamate amidohydrolase. Other names in common use include N2-succinylglutamate desuccinylase, SGDS, and AstE. This enzyme participates in arginine and proline metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Theanine%20hydrolase | In enzymology, a theanine hydrolase () is an enzyme that catalyzes the chemical reaction
N5-ethyl-L-glutamine + H2O L-glutamate + ethylamine
Thus, the two substrates of this enzyme are N5-ethyl-L-glutamine and H2O, whereas its two products are L-glutamate and ethylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N5-ethyl-L-glutamine amidohydrolase. Other names in common use include L-theanine amidohydrolase, and 5-N-ethyl-L-glutamine amidohydrolase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Thiocyanate%20hydrolase | In enzymology, a thiocyanate hydrolase () is an enzyme that catalyzes the chemical reaction
thiocyanate + 2 H2O carbonyl sulfide + NH3 + HO-
Thus, the two substrates of this enzyme are thiocyanate and H2O, whereas its 3 products are carbonyl sulfide, NH3, and HO-.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is thiocyanate aminohydrolase.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.5.5
Enzymes of known structure |
https://en.wikipedia.org/wiki/Tryptophanamidase | In enzymology, a tryptophanamidase () is an enzyme that catalyzes the chemical reaction
L-tryptophanamide + H2O L-tryptophan + NH3
Thus, the two substrates of this enzyme are L-tryptophanamide and H2O, whereas its two products are L-tryptophan and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-tryptophanamide amidohydrolase. Other names in common use include tryptophan aminopeptidase, and L-tryptophan aminopeptidase. It employs one cofactor, manganese.
References
EC 3.5.1
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ureidoglycolate%20hydrolase | In enzymology, an ureidoglycolate hydrolase () is an enzyme that catalyzes the chemical reaction
(S)-ureidoglycolate + H2O glyoxylate + 2 NH3 + CO2
Thus, the two substrates of this enzyme are (S)-ureidoglycolate and H2O, whereas its 3 products are glyoxylate, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is (S)-ureidoglycolate amidohydrolase (decarboxylating). This enzyme participates in purine metabolism.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Ureidosuccinase | In enzymology, an ureidosuccinase () is an enzyme that catalyzes the chemical reaction
N-carbamoyl-L-aspartate + H2O L-aspartate + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoyl-L-aspartate and H2O, whereas its 3 products are L-aspartate, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-aspartate amidohydrolase. This enzyme participates in alanine and aspartate metabolism.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Urethanase | In enzymology, an urethanase () is an enzyme that catalyzes the chemical reaction
urethane + H2O ethanol + CO2 + NH3
Thus, the two substrates of this enzyme are urethane and H2O, whereas its 3 products are ethanol, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urethane amidohydrolase (decarboxylating). This enzyme is also called urethane hydrolase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Stichoneuron | Stichoneuron is a genus in the family Stemonaceae erected in 1883.
Stichoneuron is native to Assam, Bangladesh, Myanmar, Thailand, and Peninsular Malaysia.
Species
Stichoneuron bognerianum Duyfjes - Johor
Stichoneuron calcicola Inthachub - southern Thailand
Stichoneuron caudatum Ridl. - Thailand, Peninsular Malaysia
Stichoneuron halabalense Inthachub - southern Thailand, Peninsular Malaysia
Stichoneuron membranaceum Hook.f. - Assam, Bangladesh, Myanmar
References
Pandanales genera
Stemonaceae
Taxa named by Joseph Dalton Hooker |
https://en.wikipedia.org/wiki/Indicator%20organism | Indicator organisms are used as a proxy to monitor conditions in a particular environment, ecosystem, area, habitat, or consumer product. Certain bacteria, fungi and helminth eggs are being used for various purposes.
Types
Indicator bacteria
Certain bacteria can be used as indicator organisms in particular situations, such as when present in bodies of water. Indicator bacteria themselves may not be pathogenic but their presence in waste may indicate the presence of other pathogens. Similar to how there are various types of indicator organisms, there are also various types of indicator bacteria. The most common indicators are total coliforms, fecal coliforms, E. coli, and enterococci. The presence of bacteria commonly found in human feces, termed coliform bacteria (e.g. E. coli), in surface water is a common indicator of faecal contamination. The means by which pathogens found in fecal matter can enter recreational bodies of water include, but are not limited to, sewage, septic systems, urban runoff, coastal recreational waste, and livestock waste.
For this reason, sanitation programs often test water for the presence of these organisms to ensure that drinking water systems are not contaminated with feces. This testing can be done using several methods which generally involve taking samples of water, or passing large amounts of water through a filter to sample bacteria, then testing to see if bacteria from that water grow on selective media such as MacConkey agar. MacConk |
https://en.wikipedia.org/wiki/Probable%20low%20affinity%20copper%20uptake%20protein%202 | Probable low affinity copper uptake protein 2 is a protein that in humans is encoded by the SLC31A2 gene.
See also
Solute carrier family
References
Further reading
Solute carrier family |
https://en.wikipedia.org/wiki/3MBS | 3MBS was the first FM (frequency modulation) radio station in Victoria, Australia, and began transmitting to Melbourne and surrounding areas on 1 July 1975. Since then it has operated successfully as a non-profit community-based organisation broadcasting classical and jazz music. 3MBS also led the way for the introduction of community radio in Australia back in 1968.
It is a part of the national Australian Fine Music Network.
History
The increasing popularity of rock music through the late '50s and '60s led to a reduction in the amount of classical music played on the ABC and commercial radio stations in Australia. Up until the early 1950s most radio stations employed orchestras to play music which included classical music. By the 1960s, only the ABC supported its own orchestra. But even the ABC had dramatically reduced the amount of classical music on air.
A music fan and radio engineer, Brian Cabena, was unhappy about being unable to listen to the music he liked on the radio - and he did something about it. After much unsuccessful lobbying of radio stations, he turned his attention to the government. He argued that if the existing stations were not willing to program for classical music fans, the government should license new stations that would.
In 1968, Cabena wrote a letter to The Age calling a meeting of anyone interested in pursuing the idea of a listener-run classical music radio station. 200 people turned up and the Music Broadcasting Society (MBS) of Victoria wa |
https://en.wikipedia.org/wiki/Kawasaki%27s%20theorem | Kawasaki's theorem or Kawasaki–Justin theorem is a theorem in the mathematics of paper folding that describes the crease patterns with a single vertex that may be folded to form a flat figure. It states that the pattern is flat-foldable if and only if alternatingly adding and subtracting the angles of consecutive folds around the vertex gives an alternating sum of zero.
Crease patterns with more than one vertex do not obey such a simple criterion, and are NP-hard to fold.
The theorem is named after one of its discoverers, Toshikazu Kawasaki. However, several others also contributed to its discovery, and it is sometimes called the Kawasaki–Justin theorem or Husimi's theorem after other contributors, Jacques Justin and Kôdi Husimi.
Statement
A one-vertex crease pattern consists of a set of rays or creases drawn on a flat sheet of paper, all emanating from the same point interior to the sheet. (This point is called the vertex of the pattern.) Each crease must be folded, but the pattern does not specify whether the folds should be mountain folds or valley folds. The goal is to determine whether it is possible to fold the paper so that every crease is folded, no folds occur elsewhere, and the whole folded sheet of paper lies flat.
To fold flat, the number of creases must be even. This follows, for instance, from Maekawa's theorem, which states that the number of mountain folds at a flat-folded vertex differs from the number of valley folds by exactly two folds. Therefore, sup |
https://en.wikipedia.org/wiki/Terry%20Humphrey | Terryal Gene Humphrey (born August 4, 1949) is an American former professional baseball player. A catcher, he appeared in 415 games played over all or parts of nine Major League Baseball seasons for the Montreal Expos (1971–1974), Detroit Tigers (1975) and California Angels (1976–1979). He threw and batted right-handed, stood tall and weighed .
Humphrey was born in Chickasha, Oklahoma, but graduated from Carson High School in Southern California and attended Los Angeles City College and the University of Nebraska–Lincoln. He was selected in the 39th round of the 1969 Major League Baseball Draft by the Expos, a first-year expansion team; pitcher Balor Moore (the Expos' top pick) and outfielder Tony Scott (71st round) were also members of that draft class. When Humphrey was recalled from minor league baseball in September 1971, he became the second product (after Moore) of the Expo farm system to reach the major leagues.
Offensive struggles characterized Humphrey's MLB career and, except for two seasons (, when he started 65 games for Montreal, and , when he started 111 games and caught in 123 contests for the Angels), he was a reserve catcher. He was traded along with Tom Walker from the Expos to the Tigers for Woodie Fryman on December 4, . He was dealt along with Leon Roberts, Gene Pentz and Mark Lemongello from the Tigers to the Houston Astros for Milt May, Dave Roberts and Jim Crawford one year later on December 6, 1975.
His finest season came with the Angels in 1977 |
https://en.wikipedia.org/wiki/Sam%20Page%20%28footballer%29 | Sam Terry Page (born 30 October 1987 in Croydon) is an English footballer who plays for Chipstead.
Career
Page was associated with Crystal Palace in his mid-teens, but started his senior career with Milton Keynes Dons in November 2006 as he made his debut for the team against Brighton & Hove Albion, in which he scored their goal in a 4–1 defeat. He had loan spells at Aylesbury United both during the 2005–06 season, and at the start of the 2006–07 season. He joined Hendon on loan in late September 2006, scoring on his debut. In February 2007 he moved to Cambridge United on a month's loan. This loan was extended until the end of the 2006–07 season in March. He returned to Hendon on a month's loan in October 2007, after a spell with Walton & Hersham. This was extended in November. In January 2008 he made an appearance in the Hillier Senior Cup for Rushden & Diamonds. Despite scoring a goal in his combined debut and final game, he failed to win an extension to the contract. Instead, a few days later he signed another loan deal with Hendon, until the end of the season. He moved on to Horsham on a 12-month contract the following season, to reduce his travelling time.
Page signed for Sutton United during the 2010 close season, and played 50 games to help the side win the 2010–11 Isthmian League Premier Division title.
On 8 June 2012 it was announced Page signed for Conference South side Havant and Waterlooville. Later moves include Staines Town in December 2018, Kingstonian in Jun |
https://en.wikipedia.org/wiki/GPR161 | G-protein coupled receptor 161 is a protein that in humans is encoded by the GPR161 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Colored-particle-in-cell | A particle in cell simulation for non-Abelian (colored) particles and fields. Can be used to simulate an equilibrium or non-equilibrium quark-gluon plasma.
References
Quantum chromodynamics |
https://en.wikipedia.org/wiki/GPR56 | G protein-coupled receptor 56 also known as TM7XN1 is a protein encoded by the ADGRG1 gene. GPR56 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR56 is expressed in liver, muscle, tendon, neural, and cytotoxic lymphoid cells in human as well as in hematopoietic precursor, muscle, and developing neural cells in the mouse.
GPR56 has been shown to have numerous role in cell guidance/adhesion as exemplified by its roles in tumour inhibition and neuron development. More recently it has been shown to be a marker for cytotoxic T cells and a subgroup of Natural killer cells.
Ligands
GPR56 binds transglutaminase 2 to suppress tumor metastasis and binds collagen III to regulate cortical development and lamination.
Signaling
GPR56 couples to Gαq/11 protein upon association with the tetraspanins CD9 and CD81. Forced GPR56 expression activates NF-kB, PAI-1, and TCF transcriptional response elements. The splicing of GPR56 induces tumorigenic responses as a result of activating the transcription of genes, such as COX2, iNOS, and VEGF85. GPR56 couples to the Gα12/13 protein and activates RhoA and mammalian target of rapamycin (mTOR) pathway upon ligand binding. Lack of the N-terminal fragment (NTF) of GPR56 causes stronger RhoA signaling and β-arrestin accumulation, leading to |
https://en.wikipedia.org/wiki/GPR83 | Probable G-protein coupled receptor 83 is a protein that in humans is encoded by the GPR83 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Sieve%20of%20Sundaram | In mathematics, the sieve of Sundaram is a variant of the sieve of Eratosthenes, a simple deterministic algorithm for finding all the prime numbers up to a specified integer. It was discovered by Indian student S. P. Sundaram in 1934.
Algorithm
Start with a list of the integers from 1 to n. From this list, remove all numbers of the form where:
The remaining numbers are doubled and incremented by one, giving a list of the odd prime numbers (i.e., all primes except 2) below .
The sieve of Sundaram sieves out the composite numbers just as the sieve of Eratosthenes does, but even numbers are not considered; the work of "crossing out" the multiples of 2 is done by the final double-and-increment step. Whenever Eratosthenes' method would cross out k different multiples of a prime , Sundaram's method crosses out for .
Correctness
If we start with integers from to , the final list contains only odd integers from to . From this final list, some odd integers have been excluded; we must show these are precisely the composite odd integers less than .
Let be an odd integer of the form . Then, is excluded if and only if is of the form , that is . Then we have:
So, an odd integer is excluded from the final list if and only if it has a factorization of the form — which is to say, if it has a non-trivial odd factor. Therefore the list must be composed of exactly the set of odd prime numbers less than or equal to .
def sieve_of_Sundaram(n):
"""The sieve of Sundaram is a si |
https://en.wikipedia.org/wiki/GPR162 | Probable G-protein coupled receptor 162 is a protein that in humans is encoded by the GPR162 gene.
This gene was identified upon genomic analysis of a gene-dense region at human chromosome 12p13. It appears to be mainly expressed in the brain; however, its function is not known. Alternatively spliced transcript variants encoding different isoforms have been identified.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR85 | Probable G-protein coupled receptor 85 is a protein that in humans is encoded by the GPR85 gene.
See also
SREB
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR139 | G-protein coupled receptor 139 (GPC139) is a protein that in humans is encoded by the GPR139 gene. Recent research ('21) has shown that mice with loss of GCP139 experience schizophrenia-like symptomatology that is rescued with the dopamine receptor antagonist haloperidol and the μ-opioid receptor antagonist naltrexone; as well, the recently developed, potent, and GPR139 receptor selective agonist TAK-041 (aka NBI-1065846) is currently undergoing trials to gauge the efficacy for treating psychiatric conditions such as major depressive disorder and the negative symptoms of schizophrenia.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR151 | Probable G-protein coupled receptor 151 is a protein that in humans is encoded by the GPR151 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Free%20fatty%20acid%20receptor%204 | Free Fatty acid receptor 4 (FFAR4), also termed G-protein coupled receptor 120 (GPR120), is a protein that in humans is encoded (i.e., its formation is directed) by the FFAR4 gene. This gene is located on the long (i.e. "P") arm of chromosome 10 at position 23.33 (position notated as 10q23.33). G protein-coupled receptors (also termed GPRs or GPCRs) reside on their parent cells' surface membranes, bind any one of the specific set of ligands that they recognize, and thereby are activated to trigger certain responses in their parent cells. FFAR4 is a rhodopsin-like GPR in the broad family of GPRs which in humans are encoded by more than 800 different genes. It is also a member of a small family of structurally and functionally related GPRs that include at least three other free fatty acid receptors (FFARs) viz., FFAR1 (also termed GPR40), FFAR2 (also termed GPR43), and FFAR3 (also termed GPR41). These four FFARs bind and thereby are activated by certain fatty acids.
FFAR4 protein is expressed in a wide range of cell types. Studies conducted primarily on human and rodent cultured cells and in animals (mostly rodents) suggest that FFAR4 acts in these cells to regulate many normal bodily functions such as food preferences, food consumption, food tastes, body weight, blood sugar (i.e., glucose) levels, inflammation, atherosclerosis, and bone remodeling. Studies also suggest that the stimulation or suppression of FFAR4 alters the development and progression of several types of can |
https://en.wikipedia.org/wiki/GPR142 | Probable G-protein coupled receptor 142 is a protein that in humans is encoded by the GPR142 gene.
GPR142 is a member of the rhodopsin family of G protein-coupled receptors (GPRs) (Fredriksson et al., 2003).[supplied by OMIM]
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR148 | G protein-coupled receptor 148, also known as GPR148, is a human orphan receptor from GPCR superfamily. It is expressed primarily in nervous system and testis. Is may be implicated in prostate cancer.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR3 | G-protein coupled receptor 3 is a protein that in humans is encoded by the GPR3 gene. The protein encoded by this gene is a member of the G protein-coupled receptor family of transmembrane receptors and is involved in signal transduction.
GPR3 mRNA is broadly expressed in neurons in various brain regions, including the cortex, thalamus, hypothalamus, amygdala, hippocampus, pituitary, and cerebellum. GPR3 mRNA is also expressed in the eye, lung, kidney, liver, testes, and ovary, among other tissues.
Individuals afflicted by Alzheimer's disease have in many cases, overexpression of the GPR3 protein in their neurons.
Function
GPR3 activates adenylate cyclase in the absence of ligand. GPR3 was first described as a constitutive activator of adenylate cyclase. This constitutive activity could be due to stimulation by a ubiquitous ligand that may be free, membrane-bound, or membrane-derived. Alternatively, they propose that this could also be due to basal Gs coupling. Various groups have since supported this initial finding of GPR3 constitutive activation and have proceeded to show similar Gs activity in GPR6 and GPR12.
GPR3 is expressed in mammalian oocytes where it maintains meiotic arrest and is thought to be a communication link between oocytes and the surrounding somatic tissue. It has been proposed that sphingosine 1-phosphate (S1P) and sphingosylphosphorylcholine (SPC) are GPR3 ligands, however this result was not confirmed in a β-arrestin recruitment assay.
Mice lacki |
https://en.wikipedia.org/wiki/Melatonin%20receptor%201B | Melatonin receptor 1B, also known as MTNR1B, is a protein that in humans is encoded by the MTNR1B gene.
Function
This gene encodes the MT2 protein, one of two high-affinity forms of a receptor for melatonin, the primary hormone secreted by the pineal gland. This gene product is an integral membrane protein that is a G-protein coupled, 7-transmembrane receptor. It is found primarily in the retina and brain; however, this detection requires RT-PCR. It is thought to participate in light-dependent functions in the retina and may be involved in the neurobiological effects of melatonin. Besides the brain and retina this receptor is expressed on the bone forming cells where it regulates their function in depositing bone.
Clinical significance
Several studies have identified MTNR1B receptor mutations that are associated with increased average blood sugar level and around a 20 percent elevated risk of developing type 2 diabetes. MTNR1B mRNA is expressed in human islets, and immunocytochemistry confirms that it is primarily localized in beta cells in islets.
Ligands
The following MT2R ligands have selectivity over MT1R:
Compound 3d: antagonist with sub-nM affinity
Compound 18f: antagonist and compound 18g partial agonist: sub-nM affinity, >100-fold selectivity over MT1
Compound 14: antagonist
Compound 13: agonist
See also
Melatonin receptor
Discovery and development of melatonin receptor agonists
References
Further reading
External links
G protein-coupled rece |
https://en.wikipedia.org/wiki/Melanin-concentrating%20hormone%20receptor%201 | Melanin-concentrating hormone receptor 1, also known as MCH1, is one of the melanin-concentrating hormone receptors found in all mammals.
The protein encoded by this gene, a member of the G protein-coupled receptor family 1, is an integral plasma membrane protein which binds melanin-concentrating hormone. The encoded protein can inhibit cAMP accumulation and stimulate intracellular calcium flux, and is probably involved in the neuronal regulation of food consumption. Although structurally similar to somatostatin receptors, this protein does not seem to bind somatostatin.
Function
MCH1 is thought to have a number of functions including in the regulation of appetite, and in stress, anxiety and depression.
Selective ligands
Agonists
Melanin concentrating hormone (MCH)
S-36057 - modified MCH 6-13 fragment substituted with 3-iodotyrosine at N-terminus via dioxyoctanoyl linker, used as 125I radioligand for mapping MCH1 in vivo.
LK-184 (Procter & Gamble) is one pick
Antagonists
ATC-0065
ATC-0175
GW-803,430
NGD-4715
SNAP-7941
SNAP-94847
T-226,296
See also
Melanin-concentrating hormone receptor
References
Further reading
External links
G protein-coupled receptors
Human proteins |
https://en.wikipedia.org/wiki/Melanin-concentrating%20hormone%20receptor%202 | Melanin-concentrating hormone receptor 2 (MCH2) also known as G-protein coupled receptor 145 (GPR145) is a protein that in humans is encoded by the MCHR2 gene.
MCH2 is also found in dogs, ferrets, and some other primates and carnivores, but is not found in mice or rats. This has delayed research into the receptor as a therapeutic target, due to most early pharmaceutical research usually being conducted in small mammals such as mice, rats or rabbits which lack the MCH2 gene and its receptor product.
Clinical significance
Treatment of human cells expressing MCHR2 with MCH resulted in upregulation of IDH3A, PCK1 and PFKFB4 and the downregulation of INSIG2 and ACOT8.
See also
Melanin-concentrating hormone receptor
References
External links
Further reading
G protein-coupled receptors
Human proteins |
https://en.wikipedia.org/wiki/Butyryl-CoA | Butyryl-coenzyme A (or butyryl-CoA) is the coenzyme A-containing derivative of butyric acid. It is acted upon by butyryl-CoA dehydrogenase and an intermediary compound of ABE fermentation.
Butyryl-CoA is a precursor to and converted from crotonyl-CoA. This interconversion is mediated by butyryl-COA dehydrogenase. FADH- is the hydride to crotonyl-CoA and FAD+ is the hydride acceptor. It is essential in reducing ferredoxins in anaerobic bacteria and archaea so that electron transport phosphorylation and substrate level phosphorylation can occur with increased efficiency.
From redox data, butyryl-COA dehydrogenase shows little to no activity at pH higher than 7.0. This is important as enzyme midpoint potential is at pH 7.0 and at 25 degrees C. Therefore, changes above from this value will denature the enzyme.
Within the human colon, butyrate helps supply energy to the gut epithelium and helps regulate cell responses.
Further reading
See also
Acyl-CoA
Fatty acyl-CoA esters
References
Thioesters of coenzyme A |
https://en.wikipedia.org/wiki/List%20of%20Caribbean%20idiophones | Historically, idiophones (percussion instruments without membranes or strings) have been widespread throughout the Caribbean music area, which encompasses the islands and coasts of the Caribbean Sea. Some areas of South America that are not geographically part of the Caribbean, but are culturally associated with its traditions, such as Guyana, Suriname, French Guiana and parts of Brazil are also taken into account.
Although some idiophones such as the mayohuacán and probably the maraca already existed among the indigenous Taíno population of the Greater Antilles before the Spanish colonization of the Americas, most idiophones were introduced in the Caribbean between the 17th and 19th centuries by enslaved Africans, which were ethnically diverse (Yoruba, Ewe, Fon, Igbo, Efik, Mandinka and Kongo, among others). Because of the different materials present in the islands, African slaves had to construct their instruments differently, and thus new instruments began to be developed.
References
Notes
Idiophones
Idiophones
Caribbean idiophones
Central American and Caribbean percussion instruments |
https://en.wikipedia.org/wiki/Oxoeicosanoid%20receptor%201 | Oxoeicosanoid receptor 1 (OXER1) also known as G-protein coupled receptor 170 (GPR170) is a protein that in humans is encoded by the OXER1 gene located on human chromosome 2p21; it is the principal receptor for the 5-Hydroxyicosatetraenoic acid family of carboxy fatty acid metabolites derived from arachidonic acid. The receptor has also been termed hGPCR48, HGPCR48, and R527 but OXER1 is now its preferred designation. OXER1 is a G protein-coupled receptor (GPCR) that is structurally related to the hydroxy-carboxylic acid (HCA) family of G protein-coupled receptors whose three members are HCA1 (GPR81), HCA2 (Niacin receptor 1), and HCA3 (Niacin receptor 2); OXER1 has 30.3%, 30.7%, and 30.7% amino acid sequence identity with these GPCRs, respectively. It is also related (30.4% amino acid sequence identity) to the recently defined receptor, GPR31, for the hydroxyl-carboxy fatty acid 12-HETE.
Species and tissue distribution
Orthologs of OXER1 are found in various mammalian species including opossums and several species of fish; however, mice and rats lack a clear ortholog of OXER1. This represents an important hindrance to studies on the function of OXER1 since these two mammalian species are the most common and easiest models for investigating the in vivo functions of receptors in mammals and by extrapolation humans. Since mouse cells make and respond to members of the 5-HETE family of agonists, it is most likely that mice do have a receptor that substitutes for OXER1 b |
https://en.wikipedia.org/wiki/Prostaglandin%20EP1%20receptor | {{DISPLAYTITLE:Prostaglandin EP1 receptor}}
Prostaglandin E2 receptor 1 (EP1) is a 42kDa prostaglandin receptor encoded by the PTGER1 gene. EP1 is one of four identified EP receptors, EP1, EP2, EP3, and EP4 which bind with and mediate cellular responses principally to prostaglandin E2) (PGE2) and also but generally with lesser affinity and responsiveness to certain other prostanoids (see Prostaglandin receptors). Animal model studies have implicated EP1 in various physiological and pathological responses. However, key differences in the distribution of EP1 between these test animals and humans as well as other complicating issues make it difficult to establish the function(s) of this receptor in human health and disease.
Gene
The PTGER1 gene is located on human chromosome 19 at position p13.12 (i.e. 19p13.12), contains 2 introns and 3 exons, and codes for a G protein-coupled receptor (GPCR) of the rhodopsin-like receptor family, Subfamily A14 (see rhodopsin-like receptors#Subfamily A14).
Expression
Studies in mice, rats, and guinea pigs have found EP1 Messenger RNA and protein to be expressed in the papillary collecting ducts of the kidney, in the kidney, lung, stomach, thalamus, and in the dorsal root ganglia neurons as well as several central nervous system sites. However, the expression of EP1 In humans, its expression appears to be more limited: EP1 receptors have been detected in human mast cells, pulmonary veins, keratinocytes, myometrium, and colon smooth muscle.
L |
https://en.wikipedia.org/wiki/Prostaglandin%20EP2%20receptor | {{DISPLAYTITLE:Prostaglandin EP2 receptor}}
Prostaglandin E2 receptor 2, also known as EP2, is a prostaglandin receptor for prostaglandin E2 (PGE2) encoded by the human gene PTGER2: it is one of four identified EP receptors, the others being EP1, EP3, and EP4, which bind with and mediate cellular responses to PGE2 and also, but with lesser affinity and responsiveness, certain other prostanoids (see Prostaglandin receptors). EP has been implicated in various physiological and pathological responses.
Gene
The PTGER2 gene is located on human chromosome 14 at position p22.1 (i.e. 14q22.1), contains 2 introns and 3 exons, and codes for a G protein coupled receptor (GPCR) of the rhodopsin-like receptor family, Subfamily A14 (see rhodopsin-like receptors#Subfamily A14).
Expression
EP2 is widely distributed in humans. Its protein is expressed in human small intestine, lung, media of arteries and arterioles of the kidney, thymus, uterus, brain cerebral cortex, brain striatum, brain hippocampus, corneal epithelium, corneal choriocapillaries, Myometriuml cells, eosinophiles, sclera of the eye, articular cartilage, the corpus cavernosum of the penis, and airway smooth muscle cells; its mRNA is expressed in gingival fibroblasts, monocyte-derived dendritic cells, aorta, corpus cavernosum of the penis, articular cartilage, airway smooth muscle, and airway epithelial cells. In rats, the receptor protein and/or mRNA has been found in lung, spleen, intestine, skin, kidney, liver, long bon |
https://en.wikipedia.org/wiki/Prostaglandin%20EP3%20receptor | {{DISPLAYTITLE:Prostaglandin EP3 receptor}}
Prostaglandin EP3 receptor (53kDa), also known as EP3, is a prostaglandin receptor for prostaglandin E2 (PGE2) encoded by the human gene PTGER3; it is one of four identified EP receptors, the others being EP1, EP2, and EP4, all of which bind with and mediate cellular responses to PGE2 and also, but generally with lesser affinity and responsiveness, certain other prostanoids (see Prostaglandin receptors). EP has been implicated in various physiological and pathological responses.
Gene
The PTGER3 gene is located on human chromosome 1 at position p31.1 (i.e. 1p31.1), contains 10 exons, and codes for a G protein coupled receptor (GPCR) of the rhodopsin-like receptor family, Subfamily A14 (see rhodopsin-like receptors#Subfamily A14). PTGER3 codes for at least 8 different isoforms in humans, i.e. PTGER3-1 to PGGER3-8 (i.e., EP3-1, EP3-2, EP3-3, EP3-4, EP3-5, EP3-6, EP3-7, and EP3-8), while Ptger3 codes for at least 3 isoforms in mice, Ptger1-Ptger3 (i.e. Ep3-α, Ep3-β, and Ep3-γ). These isoforms are variants made by Alternative splicing conducted at the 5'-end of DNA to form proteins that vary at or near their C-terminus. Since these isoforms different in their tissue expressions as well as the signaling pathways which they activate, they may vary in the functions that they perform. Further studies are needed to examine functional differences among these isoforms.
Expression
EP3 is widely distributed in humans. Its protein and/or mRNA |
https://en.wikipedia.org/wiki/Australian%20Wildlife%20Conservancy | The Australian Wildlife Conservancy (AWC) is an Australian independent, nonprofit organisation, working to conserve threatened wildlife and ecosystems in Australia. This is principally achieved through the acquisition of extensive areas of land on which to establish conservation reserves ("sanctuaries") or by entering into partnerships with government, Indigenous groups, and private landholders to manage landscapes for effective conservation. AWC is the largest private owner and manager of land for conservation in Australia, currently managing 31 sanctuaries and partnership sites for wildlife conservation that cover over 6.5 million hectares of land across Australia.
Australian Wildlife Conservancy operates under a unique model for conservation, using science (predominantly biodiversity survey work and targeted research) to inform on-ground land management, such as control of fire, feral animals and weeds. There is a strong focus on wildlife conservation: consequently, about 80% of all staff are based in the field and, as of 2021, 83.5% of AWC's total expenditure is invested into conservation programs.
Most funding comes from private support in the form of tax-deductible donations from the public, as well as some government grants for particular purposes, such as from the Australian government's National Reserve System Program.
Australian Wildlife Conservancy was founded in response to Australia's mammal extinction crisis. Over a third of the world's extinctions from the l |
https://en.wikipedia.org/wiki/MAS1L | Mas-related G-protein coupled receptor MRG is a protein that in humans is encoded by the MAS1L gene.
See also
MAS1 oncogene
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Neuromedin%20U%20receptor%201 | Neuromedin-U receptor 1 is a protein that in humans is encoded by the NMUR1 gene.
See also
Neuromedin U receptor
Limostatin
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Neuromedin%20U%20receptor%202 | Neuromedin-U receptor 2 is a protein that in humans is encoded by the NMUR2 gene.
Ligands
Agonists
synephrine
See also
Neuromedin U receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Pancreatic%20polypeptide%20receptor%201 | Pancreatic polypeptide receptor 1, also known as Neuropeptide Y receptor type 4, is a protein that in humans is encoded by the PPYR1 gene.
Selective Ligands
Agonists
Pancreatic polypeptide
Neuropeptide Y (endogenous agonist, non subtype selective)
Peptide YY
GR-231,118 (mixed NPY1 antagonist / NPY4 agonist, CAS# 158859-98-4)
Antagonists
UR-AK49
See also
Neuropeptide Y receptor
References
External links
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Moonlight%20Resonance | Moonlight Resonance (Traditional Chinese: 溏心風暴之家好月圓) is a 2008 grand production HDTV drama by TVB. It is a spiritual sequel to 2007's award-winning series, Heart of Greed featuring most of the original cast members. The series is written and edited by Cheung Wah-biu and Sit Ga-wah. Sponsored by Kee Wah Bakery, the series began broadcast on 28 July 2008. It stars Louise Lee, Ha Yu, Michelle Yim, Susanna Kwan, Moses Chan, Raymond Lam and Linda Chung. Its final episode was one of the highest rated TVB episodes in the 2000s decade at 50 points. The series was met with critical acclaim, with praise to the intense plot, excellent performances by the cast, and moving storyline. It went on to receive various awards and is one of the highest-rated TVB series in viewership in the 2000s.
Plot
Chung Siu-Hor, discovered that her husband Gan Tai-Cho was having an affair with their employee Yan-Hung. Siu-Hor and Tai-Cho owned a confectionery together known as the Moonlight Bakery. Yan-Hung forces Siu-Hor and Tai-Cho to declare divorce.
After this divorce, Yan-Hung and Tai-Cho take on the Moonlight Bakery name and prove successful, resulting in a family asset totaling HK$1 billion. Meanwhile, Siu-Hor struggles to make a living at the modest bakery she once owned with Tai-Cho. Over the next ten years, Yan-Hung manipulates the family to keep relations hostile.
When Yan-Hung has a miscarriage with Tai-Cho's baby, she blames Wing-Yuen to make him feel indebted to her. Meanwhile, Siu-Hor's si |
https://en.wikipedia.org/wiki/Neurotensin%20receptor%201 | Neurotensin receptor type 1 is a protein that in humans is encoded by the NTSR1 gene. For a crystal structure of NTS1, see pdb code 4GRV. In addition, high-resolution crystal structures have been determined in complex with the peptide full agonist NTS8-13, the non-peptide full agonist SRI-9829, the partial agonist RTI-3a, and the antagonists / inverse agonists SR48692 and SR142948A, as well as in the ligand-free apo state., see PDB codes 6YVR (NTSR1-H4X:NTS8–13), 6Z4V (NTSR1-H4bmX:NTS8–13), 6Z8N (NTSR1-H4X:SRI-9829), 6ZA8 (NTSR1-H4X:RTI-3a), 6Z4S (NTSR1-H4bmX:SR48692), 6ZIN (NTSR1-H4X:SR48692), 6Z4Q (NTSR1-H4X: SR142948A), and 6Z66 (apo NTSR1-H4X).
Function
Neurotensin receptor 1, also called NTR1, belongs to the large superfamily of G-protein coupled receptors and is considered a class-A GPCR. NTSR1 mediates multiple biological processes through modulation by neurotensin, such as low blood pressure, high blood sugar, low body temperature, antinociception, anti-neuronal damage and regulation of intestinal motility and secretion.
Ligands
ML314 – β-arrestin biased agonist
Neurotensin (NT1)
See also
Neurotensin receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Canopy%20clustering%20algorithm | The canopy clustering algorithm is an unsupervised pre-clustering algorithm introduced by Andrew McCallum, Kamal Nigam and Lyle Ungar in 2000. It is often used as preprocessing step for the K-means algorithm or the Hierarchical clustering algorithm. It is intended to speed up clustering operations on large data sets, where using another algorithm directly may be impractical due to the size of the data set.
Description
The algorithm proceeds as follows, using two thresholds (the loose distance) and (the tight distance), where .
Begin with the set of data points to be clustered.
Remove a point from the set, beginning a new 'canopy' containing this point.
For each point left in the set, assign it to the new canopy if its distance to the first point of the canopy is less than the loose distance .
If the distance of the point is additionally less than the tight distance , remove it from the original set.
Repeat from step 2 until there are no more data points in the set to cluster.
These relatively cheaply clustered canopies can be sub-clustered using a more expensive but accurate algorithm.
An important note is that individual data points may be part of several canopies. As an additional speed-up, an approximate and fast distance metric can be used for 3, where a more accurate and slow distance metric can be used for step 4.
Applicability
Since the algorithm uses distance functions and requires the specification of distance thresholds, its applicability for high-dimens |
https://en.wikipedia.org/wiki/Standards%20of%20Fundamental%20Astronomy | The Standards of Fundamental Astronomy (SOFA) software libraries are a collection of subroutines that implement official International Astronomical Union (IAU) algorithms for astronomical computations.
As of February 2009 they are available in both Fortran and C source code format.
Capabilities
The subroutines in the libraries cover the following areas:
Calendars
Time scales
Earth's rotation and sidereal time
Ephemerides (limited precision)
Precession, nutation, polar motion
Proper motion
Star catalog conversions
Astrometric transformations
Galactic Coordinates
Licensing
As of the February 2009 release, SOFA licensing changed to allow use for any purpose, provided certain requirements are met. Previously, commercial usage was specifically excluded and required written agreement of the SOFA board.
See also
Naval Observatory Vector Astrometry Subroutines
References
External links
SOFA Home Page
Scholarpedia overview of SOFA
International Astronomical Union and Working group "Standards of Fundamental Astronomy
Celestial mechanics
Astronomical coordinate systems
Numerical software
Astronomy software |
https://en.wikipedia.org/wiki/Hakaluki%20Haor | Hakaluki Haor () is a marsh wetland ecosystem of north-eastern Bangladesh. It is one of Bangladesh's largest and one of Asia's large marsh wetland resources. Hakaluki Haor is bounded by the Kushiara river as well as a part of the Sonai Bardal river to the north, by the Fenchuganj-Kulaura railway to the west and to the south, and by the Kulaura-Beanibazar road the east. It lies between 24°35’ N to 24°44’ N and 92°00’ E to 92°08’ E.
A total of 558 species of animals and birds have been identified here, including some very rare – already declared as threatened, vulnerable, endangered and critically endangered species. Some 190,000 people live in the surrounding Hakaluki haor area.
Hakaluki Haor was designated an Ecologically Critical Area (ECA).
The surface area of Hakaluki Haor is 181.15 km2, of which 72.46 km2 (40.01%) is within the territory of Barlekha Upazila. It is also under Kulaura Juri upazila of Moulvibazar District and Golapganj, Fenchuganj upazila of Sylhet district.
See also
Haor
Fenchuganj Upazila
References
Marshes of Bangladesh
Beanibazar Upazila
Barlekha Upazila
Fenchuganj Upazila
Juri Upazila
Golapganj Upazila
Kulaura Upazila |
https://en.wikipedia.org/wiki/P2RY4 | P2Y purinoceptor 4 is a protein that in humans is encoded by the P2RY4 gene.
The product of this gene, P2Y4, belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor is responsive to uridine nucleotides, partially responsive to ATP, and not responsive to ADP.
See also
P2Y receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Structural%20break | In econometrics and statistics, a structural break is an unexpected change over time in the parameters of regression models, which can lead to huge forecasting errors and unreliability of the model in general. This issue was popularised by David Hendry, who argued that lack of stability of coefficients frequently caused forecast failure, and therefore we must routinely test for structural stability. Structural stability − i.e., the time-invariance of regression coefficients − is a central issue in all applications of linear regression models.
Structural break tests
A single break in mean with a known breakpoint
For linear regression models, the Chow test is often used to test for a single break in mean at a known time period for . This test assesses whether the coefficients in a regression model are the same for periods and .
Other forms of structural breaks
Other challenges occur where there are:
Case 1: a known number of breaks in mean with unknown break points;
Case 2: an unknown number of breaks in mean with unknown break points;
Case 3: breaks in variance.
The Chow test is not applicable in these situations, since it only applies to models with a known breakpoint and where the error variance remains constant before and after the break. Bayesian methods exist to address these difficult cases via Markov chain Monte Carlo inference.
In general, the CUSUM (cumulative sum) and CUSUM-sq (CUSUM squared) tests can be used to test the constancy of the coefficients in a |
https://en.wikipedia.org/wiki/SPAH | SPAH can be an abbreviation for:
The Society for the Preservation and Advancement of the Harmonica
Stacked pairs of alpha helices, a term for the alpha solenoid protein fold |
https://en.wikipedia.org/wiki/Relaxin/insulin-like%20family%20peptide%20receptor%202 | Relaxin/insulin-like family peptide receptor 2, also known as RXFP2, is a human G-protein coupled receptor.
The receptors for glycoprotein hormones such as follicle-stimulating hormone (FSH; see MIM 136530) and thyroid-stimulating hormone (TSH; see MIM 188540) are G protein-coupled, 7-transmembrane receptors (GPCRs) with large N-terminal extracellular domains. Leucine-rich repeat (LRR)-containing GPCRs (LGRs) form a subgroup of the GPCR superfamily. [supplied by OMIM].
See also
Relaxin receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR50 | G protein-coupled receptor 50 is a protein which in humans is encoded by the GPR50 gene.
Function
GPR50 is a member of the G protein-coupled receptor family of integral membrane proteins and is most closely related to the melatonin receptor. GPR50 is able to heterodimerize with both the MT1 and MT2 melatonin receptor subtypes. While GPR50 has no effect on MT2 function, GPR50 prevented MT1 from both binding
melatonin and coupling to G proteins. GPR50 is the mammalian ortholog of melatonin receptor Mel1c described in non-mammalian vertebrates.
Clinical significance
Certain polymorphisms of the GPR50 gene in females are associated with increased risk of developing bipolar affective disorder, major depressive disorder, and schizophrenia. Other GPR50 gene polymorphism are associated with higher fasting circulating triglyceride levels and lower circulating High-density lipoprotein levels.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Homojunction | A homojunction is a semiconductor interface that occurs between layers of similar semiconductor material; these materials have equal band gaps but typically have different doping. In most practical cases a homojunction occurs at the interface between an n-type (donor doped) and p-type (acceptor doped) semiconductor such as silicon, this is called a p–n junction.
This is not a necessary condition as the only requirement is that the same semiconductor (same band gap) is found on both sides of the junction, in contrast to a heterojunction. An n-type to n-type junction, for example, would be considered a homojunction even if the doping levels are different.
The different doping level will cause band bending, and a depletion region will be formed at the interface, as shown in the figure to the right.
See also
Transistor
p–n junction
Band bending
Doping (semiconductor)
Semiconductor structures |
https://en.wikipedia.org/wiki/Parth%C3%A9ite | Partheite or parthéite is a calcium aluminium silicate and a member of the zeolite group of minerals, a group of silicates with large open channels throughout the crystal structure, which allow passage of liquids and gasses through the mineral. It was first discovered in 1979 in rodingitic dikes in an ophiolite zone of the Taurus Mountains in southwest Turkey. The second discovery occurred in gabbro-pegmatites in the Ural Mountains, Russia. Since its discovery and naming, the chemical formula for partheite has been revised from CaAl2Si2O8•2H2O to include not only water but hydroxyl groups as well. The framework of the mineral is interrupted due to these hydroxyl groups attaching themselves to aluminum centered oxygen tetrahedra. This type of interrupted framework is known in only one other zeolite, the mineral roggianite. As a silicate based mineral with the properties of a zeolite, partheite was first described as zeolite-like in 1984 and listed as a zeolite in 1985. Partheite and lawsonite are polymorphs. Associated minerals include prehnite, thomsonite, augite, chlorite and tremolite.
Composition
Partheite is a calcium alumino-silicate with the chemical formula Ca2Al4Si4O15(OH)2∙4(H2O). This is a revised version of the formula reported initially as CaAl2Si2O8•2(H2O) that was determined using electron microprobe analysis. A new formula was necessary after structural analysis revealed the presence of hydroxyl groups in the structure. This new formula fell within the error l |
https://en.wikipedia.org/wiki/Diduga | Diduga is a genus of moths in the family Erebidae.
Description
Palpi slender and obliquely porrect. Tibia with long spurs. Forewings with vein 3 arise from before angle of cell. Veins 4 and 5 from angle, vein 6 from upper angle and veins 7 and 8 are stalked. Hindwings with vein 4 from angle of cell, vein 5 from above angle, vein 3 absent and veins 6 and 7 are stalked. Forewings of male possess a costal fold acting like the retinaculum.
Species
Diduga albicosta
Diduga albida
Diduga annulata
Diduga barlowi
Diduga ciliata
Diduga dorsolobata
Diduga excisa
Diduga flavicostata
Diduga fumipennis
Diduga haematomiformis
Diduga metaleuca
Diduga pectinifer
Diduga plumosa
Diduga rufidiscalis
Diduga trichophora
References
External links
Nudariina
Moth genera |
https://en.wikipedia.org/wiki/Dodia | Dodia is a genus of woolly bear moths in the family Erebidae. The genus was erected by Harrison Gray Dyar Jr. in 1901. The moths are found in subarctic tundra and taiga ecosystems. They belong to the subtribe Callimorphina of tribe Arctiini.
Like most of their closest relatives, they are mid-sized moths (a few cm/around 1 inch wingspan) which may be active all day, but avoid direct sunlight. Unlike many of the Callimorphina, they are inconspicuous and coloured a somewhat translucent grey-brown and without bold markings. They have the typical slender body shape of other species of their subtribe, and they resemble, at a casual glance, certain larentiine geometer moths (Geometridae), e.g. the Operophterini, rather than the more typical Callimorphina. Like in the former, flightless females are known to occur in Dodia.
Species
Long held to contain only two species, several more have been discovered and described since the 1980s. Consequently, it is quite possible that further species await discovery. As of 2009, the known species are:
Dodia albertae Dyar, 1901
Dodia diaphana (Eversmann, 1848)
Dodia kononenkoi Tshistjakov & Lafontaine, 1984
Dodia maja Rekelj & Česanek, 2009
Dodia sazonovi Dubatolov, 1990
Dodia tarandus Schmidt et Macaulay, 2009
Dodia transbaikalensis Tshistjakov, 1988 (sometimes in D. kononenkoi)
Dodia verticalis Lafontaine & Troubridge, [2000] 1999
Footnotes
References
Rekelj, J. & Česanek, M. (2009). "Dodia maja sp. n., a new tiger moth from the Mag |
https://en.wikipedia.org/wiki/Coincidence%20detection%20in%20neurobiology | Coincidence detection is a neuronal process in which a neural circuit encodes information by detecting the occurrence of temporally close but spatially distributed input signals. Coincidence detectors influence neuronal information processing by reducing temporal jitter and spontaneous activity, allowing the creation of variable associations between separate neural events in memory. The study of coincidence detectors has been crucial in neuroscience with regards to understanding the formation of computational maps in the brain.
Principles of coincidence detection
Coincidence detection relies on separate inputs converging on a common target. For example (Fig. 1), in a basic neural circuit with two input neurons—A and B—that have excitatory synaptic terminals converging on a single output neuron (C), if each input neuron's EPSP is sub-threshold for an action potential at C, then C cannot fire unless the two inputs from A and B are temporally close. The synchronous arrival of these two inputs may push the membrane potential of a target neuron over the threshold required to create an action potential. Conversely, if the two inputs temporally arrive too far apart, the depolarization of the first input may have time to drop significantly, preventing the membrane potential of the target neuron from reaching the action potential threshold. Hence, the function of coincidence detection is to reduce the jitter caused by spontaneous neuronal activity, and while random sub-threshold sti |
https://en.wikipedia.org/wiki/Anapatetris | Anapatetris is a genus of moths in the family Gelechiidae. It contains the species Anapatetris crystallista, which is found in Gauteng, South Africa.
The wingspan is about 10 mm. The forewings are white, sprinkled with black specks suffused with brownish, especially along the costa and dorsum and on two longitudinal streaks in the disc above and below middle, the upper extending from the base to three-quarters, the lower shorter, and three longitudinal marks before and beyond the tornus and at the apex. The hindwings are light grey.
References
Endemic moths of South Africa
Apatetrinae
Taxa named by Edward Meyrick
Monotypic moth genera
Moths of Africa
Gelechiidae genera |
https://en.wikipedia.org/wiki/Command%20neuron | A command neuron is a single neuron (or small set of neurons) whose stimulation results in the evocation of an endogenous, specific, naturally occurring behavior pattern. Command neurons act as neural decision making cells; push buttons that can trigger a complete, coordinated behavioral act and are often the sole determinant of whether an action is performed or not. Command neurons receive a convergence of integrative and sensory input and output to a multifarious group of pattern generating efferent cells. Stimulation of the command neuron triggers a lower level central pattern generator whose motorneurons and interneurons produce a particular fixed action pattern.
History
The term command neuron first appeared in a 1964 paper titled "Interneurons Commanding Swimmeret Movements in the Crayfish", by CAG Wiersma and K Ikeda in volume 12 of Comparative Biochemistry and Physiology vol 12 on pp 509–525 Wiersma and Ikeda used the term to describe how a single action potential in any of the four giant fibers that run along the dorsal margin of the crayfish nerve cord caused the crayfish to execute a tail-flip escape response. This concept came to epitomize the general neurobiological principle that complex information can be encoded on the level of individual neurons. Soon, researchers were finding command neurons in multiple invertebrate and vertebrate species, including crickets, cockroaches, lobsters, and certain fish.
Criticism
In 1978, Kupfermann and Weiss' "The Command N |
https://en.wikipedia.org/wiki/Josue%20%28footballer%2C%20born%201987%29 | Josue Souza Santos, or simply Josue (born July 10, 1987), is a Brazilian striker. Since June 2012 he has played for A.D. San Carlos.
Club statistics
References
External links
1987 births
Living people
Brazilian men's footballers
Brazilian expatriate men's footballers
Anagennisi Karditsa F.C. players
Expatriate men's footballers in Japan
J2 League players
Sagan Tosu players
FC Machida Zelvia players
Men's association football midfielders |
https://en.wikipedia.org/wiki/Kim%20Sang-woo%20%28footballer%2C%20born%201987%29 | Kim-Sang Woo (born May 18, 1987 in Jinju) is a South Korean midfielder. He currently plays for Gimhae City FC.
Club statistics
References
External links
1987 births
Living people
South Korean men's footballers
South Korean expatriate men's footballers
J2 League players
Tokushima Vortis players
Korea National League players
Expatriate men's footballers in Japan
South Korean expatriate sportspeople in Japan
Men's association football midfielders
People from Jinju
Footballers from South Gyeongsang Province |
https://en.wikipedia.org/wiki/VIPR1 | Vasoactive intestinal polypeptide receptor 1 also known as VPAC1, is a protein, that in humans is encoded by the VIPR1 gene. VPAC1 is expressed in the brain (cerebral cortex, hippocampus, amygdala), lung, prostate, peripheral blood leukocytes, liver, small intestine, heart, spleen, placenta, kidney, thymus and testis.
Function
VPAC1 is a receptor for vasoactive intestinal peptide (VIP), a small neuropeptide. Vasoactive intestinal peptide is involved in smooth muscle relaxation, exocrine and endocrine secretion, and water and ion flux in lung and intestinal epithelia. Its actions are effected through integral membrane receptors associated with a guanine nucleotide binding protein which activates adenylate cyclase.
VIP acts in an autocrine fashion via VPAC11 to inhibit megakaryocyte proliferation and induce proplatelet formation.
Clinical significance
Patients with idiopathic achalasia show a significant difference in the distribution of SNPs affecting VIPR1.
VIP and PACAP levels were decreased in anterior vaginal wall of stress urinary incontinence and pelvic organ prolapse patients, they may participate in the pathophysiology of these diseases.
See also
Vasoactive intestinal peptide receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Organic%20acidemia | Organic acidemia is a term used to classify a group of metabolic disorders which disrupt normal amino acid metabolism, particularly branched-chain amino acids, causing a buildup of acids which are usually not present.
The branched-chain amino acids include isoleucine, leucine and valine. Organic acids refer to the amino acids and certain odd-chained fatty acids which are affected by these disorders.
The four main types of organic acidemia are: methylmalonic acidemia, propionic acidemia, isovaleric acidemia, and maple syrup urine disease.
Cause
Most of the organic acidemias result from defective autosomal genes for various enzymes important to amino acid metabolism. Neurological and physiological harm is caused by this impaired ability to synthesize a key enzyme required to break down a specific amino acid, or group of amino acids, resulting in acidemia and toxicity to specific organs systems. Most are inherited as autosomal recessive diseases.
Diagnosis
Organic acidemias are usually diagnosed in infancy, characterized by urinary excretion of abnormal amounts or types of organic acids. The diagnosis is usually made by detecting an abnormal pattern of organic acids in a urine sample by gas chromatography-mass spectrometry. In some conditions, the urine is always abnormal, in others the characteristic substances are only present intermittently. Many of the organic acidemias are detectable by newborn screening with tandem mass spectrometry.
These disorders vary in their prog |
https://en.wikipedia.org/wiki/Wally%20Smith%20%28mathematician%29 | Walter Laws Smith (November 12, 1926 – March 6, 2023) was a British-born American mathematician, known for his contributions to applied probability theory.
Biography
Smith was born in London on November 12, 1926.
Smith received a B.A. in mathematics (1947) from Cambridge University, having gained First Class in the Mathematical Tripos Part 1 and Part 2. He then received an M.A. (1951) and Ph.D (1953) from Cambridge. His dissertation was entitled Stochastic Sequences of Events advised by Henry Daniels and D. R. Cox, with whom he published the book Queues (1961) and also published with in his early years. He became a professor of statistics at The University of North Carolina Chapel Hill (1954–56 and 1958–), and he was an emeritus professor in the Department of Statistics and Operations Research.
Smith was a fellow of the Institute of Mathematical Statistics, a fellow of the American Statistical Association (1966), a winner of the Adams Prize at the University of Cambridge (1960), a Sir Winston Churchill overseas fellow and a recipient of a Guggenheim Fellowship (see List of Guggenheim Fellowships awarded in 1974)
Smith died in Chapel Hill, North Carolina, on March 6, 2023, at the age of 96.
Publications
The superimposition of several strictly periodic sequences of events, in Biometrika, 40(?), 1953. With Cox.
A direct proof of a fundamental theorem of renewal theory, in Skandinavisk Aktuartidsskrift, 36(?), 1953
On the superposition of renewal processes, in Biometrika, 4 |
https://en.wikipedia.org/wiki/Vitamin%20B12 | Vitamin B12, also known as cobalamin, is a water-soluble vitamin involved in metabolism. It is one of eight B vitamins. It is required by animals, which use it as a cofactor in DNA synthesis, and in both fatty acid and amino acid metabolism. It is important in the normal functioning of the nervous system via its role in the synthesis of myelin, and in the circulatory system in the maturation of red blood cells in the bone marrow. Plants do not need cobalamin and carry out the reactions with enzymes that are not dependent on it.
Vitamin B12 is the most chemically complex of all vitamins, and for humans, the only vitamin that must be sourced from animal-derived foods or supplements. Only some archaea and bacteria can synthesize vitamin B12. Most people in developed countries get enough B12 from the consumption of meat or foods from animal sources. Foods containing vitamin B12 include meat, clams, liver, fish, poultry, eggs, and dairy products. Many breakfast cereals are fortified with the vitamin. Supplements and medications are available to treat and prevent vitamin B12 deficiency. They are taken by mouth, but for the treatment of deficiency may also be given as an intramuscular injection.
The most common cause of vitamin B12 deficiency in developed countries is impaired absorption due to a loss of gastric intrinsic factor (IF) which must be bound to a food-source of B12 in order for absorption to occur. A second major cause is an age-related decline in stomach acid producti |
https://en.wikipedia.org/wiki/Kalirin | Kalirin, also known as Huntingtin-associated protein-interacting protein (HAPIP), protein duo (DUO), or serine/threonine-protein kinase with Dbl- and pleckstrin homology domain, is a protein that in humans is encoded by the KALRN gene. Kalirin was first identified in 1997 as a protein interacting with huntingtin-associated protein 1. Is also known to play an important role in nerve growth and axonal development.
Kalirin is a member of the Dbl family of proteins and is a Rho guanine nucleotide exchange factor.
It is named after the multiple-handed Hindu goddess Kali for its ability to interact with numerous other proteins. Kalirin's other name, DUO, comes from the fact that it is 98% identical to rat DUO protein and 80.6% identical to a human protein named TRIO. Unlike TRIO, which is expressed in numerous tissues, Kalirin isoforms are mainly found in the brain.
Clinical significance
Several isoforms of Kalirin are produced through alternative splicing. One of the isoforms, Kalirin-7, was found to be necessary for the remodeling of synapses in mature cortical neurons and is thought to be important in the development of schizophrenia, as demonstrated by adolescent development of schizophrenia-like symptoms in kalirin knockout mice. Alzheimer's disease may also be linked to kalirin-7.
The KALRN gene, has been linked to multiple neurological disorders both through large exome and genome sequencing efforts, as well as post mortem and clinical studies.
Several mutations withi |
https://en.wikipedia.org/wiki/Polar%20cell | Polar cell may refer to:
Polar cells, a constituent of atmospheric circulation
Polar body, a smaller cell by-product of egg formation in some animal species |
https://en.wikipedia.org/wiki/Disease%20diffusion%20mapping | Disease diffusion occurs when a disease is transmitted to a new location. It implies that a disease spreads, or pours out, from a central source. The idea of showing the spread of disease using a diffusion pattern is relatively modern, compared to earlier methods of mapping disease, which are still used today. According to Rytokonen, the goals of disease mapping are: 1) to describe the spatial variation in disease incidence to formulate an etiological hypothesis; 2) to identify areas of high risk in order to increase prevention; and 3) to provide a map of disease risk for a region for better risk preparedness.
Torsten Hägerstrand’s early work on “waves of innovation” is the basis that many medical cartographers and geographers use for mapping spatial diffusion (1968). The diffusion of disease can be described in four patterns: expansion diffusion, contagious diffusion, hierarchal diffusion and relocation diffusion. Cromley and McLafferty also mention network diffusion and mixed diffusion.
The diffusion of infectious disease tends to occur in a ‘wave’ fashion, spreading from a central source. Pyle mentions barriers that pose a resistance towards a wave of diffusion, which include but are not limited to: physiographic features (i.e. mountains, water bodies), political boundaries, linguistic barriers, and with diseases, a barrier could be differing control programs. The diffusion of disease can be identified as a normal distribution over time and translated into an S-sh |
https://en.wikipedia.org/wiki/10-deacetylbaccatin%20III%2010-O-acetyltransferase | In enzymology, a 10-deacetylbaccatin III 10-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 10-deacetylbaccatin III CoA + baccatin III
Thus, the two substrates of this enzyme are acetyl-CoA and 10-deacetylbaccatin III, whereas its two products are CoA and baccatin III.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:taxan-10beta-ol O-acetyltransferase. This enzyme participates in diterpenoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/10-hydroxytaxane%20O-acetyltransferase | In enzymology, a 10-hydroxytaxane O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 10-desacetyltaxuyunnanin C CoA + taxuyunnanin C
Thus, the two substrates of this enzyme are acetyl-CoA and 10-desacetyltaxuyunnanin C, whereas its two products are CoA and taxuyunnanin C.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:taxan-10beta-ol O-acetyltransferase. This enzyme is also called acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/13-hydroxylupinine%20O-tigloyltransferase | In enzymology, a 13-hydroxylupinine O-tigloyltransferase () is an enzyme that catalyzes the chemical reaction
(E)-2-methylcrotonoyl-CoA + 13-hydroxylupinine CoA + 13-(2-methylcrotonoyl)oxylupinine
Thus, the two substrates of this enzyme are (E)-2-methylcrotonoyl-CoA and 13-hydroxylupinine, whereas its two products are CoA and 13-(2-methylcrotonoyl)oxylupinine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is (E)-2-methylcrotonoyl-CoA:13-hydroxylupinine O-2-methylcrotonoyltransferase. Other names in common use include tigloyl-CoA:13-hydroxylupanine O-tigloyltransferase, and 13-hydroxylupanine acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-acylglycerol-3-phosphate%20O-acyltransferase | In enzymology, a 1-acylglycerol-3-phosphate O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are acyl-CoA and 1-acyl-sn-glycerol 3-phosphate, whereas its two products are CoA and 1,2-diacyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase. Other names in common use include 1-acyl-sn-glycero-3-phosphate acyltransferase, 1-acyl-sn-glycerol 3-phosphate acyltransferase, 1-acylglycero-3-phosphate acyltransferase, 1-acylglycerolphosphate acyltransferase, 1-acylglycerophosphate acyltransferase, and lysophosphatidic acid-acyltransferase. This enzyme participates in 3 metabolic pathways: glycerolipid metabolism, glycerophospholipid metabolism, and ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-acylglycerophosphocholine%20O-acyltransferase | In enzymology, a 1-acylglycerophosphocholine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine CoA + 1,2-diacyl-sn-glycero-3-phosphocholine
Thus, the two substrates of this enzyme are acyl-CoA and 1-acyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and 1,2-diacyl-sn-glycero-3-phosphocholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Other names in common use include lysolecithin acyltransferase, 1-acyl-sn-glycero-3-phosphocholine acyltransferase, acyl coenzyme A-monoacylphosphatidylcholine acyltransferase, acyl-CoA:1-acyl-glycero-3-phosphocholine transacylase, lysophosphatide acyltransferase, and lysophosphatidylcholine acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-alkenylglycerophosphocholine%20O-acyltransferase | In enzymology, a 1-alkenylglycerophosphocholine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-alkenylglycerophosphocholine CoA + 1-alkenyl-2-acylglycerophosphocholine
Thus, the two substrates of this enzyme are acyl-CoA and 1-alkenylglycerophosphocholine, whereas its two products are CoA and 1-alkenyl-2-acylglycerophosphocholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-alkenylglycerophosphocholine O-acyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-alkenylglycerophosphoethanolamine%20O-acyltransferase | In enzymology, a 1-alkenylglycerophosphoethanolamine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-alkenylglycerophosphoethanolamine CoA + 1-alkenyl-2-acylglycerophosphoethanolamine
Thus, the two substrates of this enzyme are acyl-CoA and 1-alkenylglycerophosphoethanolamine, whereas its two products are CoA and 1-alkenyl-2-acylglycerophosphoethanolamine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-alkenylglycerophosphoethanolamine O-acyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-alkyl-2-acetylglycerol%20O-acyltransferase | In enzymology, a 1-alkyl-2-acetylglycerol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol CoA + 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol
Thus, the two substrates of this enzyme are acyl-CoA and 1-O-alkyl-2-acetyl-sn-glycerol, whereas its two products are CoA and 1-O-alkyl-2-acetyl-3-acyl-sn-glycerol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-O-alkyl-2-acetyl-sn-glycerol O-acyltransferase. This enzyme is also called 1-hexadecyl-2-acetylglycerol acyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-alkylglycerophosphocholine%20O-acetyltransferase | In enzymology, a 1-alkylglycerophosphocholine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine
Thus, the two substrates of this enzyme are acetyl-CoA and 1-alkyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:1-alkyl-sn-glycero-3-phosphocholine 2-O-acetyltransferase. Other names in common use include acetyl-CoA:1-alkyl-2-lyso-sn-glycero-3-phosphocholine, 2-O-acetyltransferase, acetyl-CoA:lyso-PAF acetyltransferase, 1-alkyl-2-lysolecithin acetyltransferase, acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine acyltransferase, blood platelet-activating factor acetyltransferase, lyso-GPC:acetyl CoA acetyltransferase, lyso-platelet activating factor:acetyl-CoA acetyltransferase, lysoPAF:acetyl CoA acetyltransferase, PAF acetyltransferase, platelet-activating factor acylhydrolase, platelet-activating factor-synthesizing enzyme, 1-alkyl-2-lyso-sn-glycero-3-phosphocholine acetyltransferase, and lyso-platelet-activating factor:acetyl-CoA acetyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/1-alkylglycerophosphocholine%20O-acyltransferase | In enzymology, a 1-alkylglycerophosphocholine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine CoA + 2-acyl-1-alkyl-sn-glycero-3-phosphocholine
Thus, the two substrates of this enzyme are acyl-CoA and 1-alkyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and 2-acyl-1-alkyl-sn-glycero-3-phosphocholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:1-alkyl-sn-glycero-3-phosphocholine O-acyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2%2C3%2C4%2C5-tetrahydropyridine-2%2C6-dicarboxylate%20N-succinyltransferase | In enzymology, a 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O CoA + N-succinyl-L-2-amino-6-oxoheptanedioate
The 3 substrates of this enzyme are succinyl-CoA, (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and H2O, whereas its two products are CoA and N-succinyl-L-2-amino-6-oxoheptanedioate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. Other names in common use include tetrahydropicolinate succinylase, tetrahydrodipicolinate N-succinyltransferase, tetrahydrodipicolinate succinyltransferase, succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase, succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, and N-succinyltransferase. This enzyme participates in lysine biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/2%2C3-diaminopropionate%20N-oxalyltransferase | In enzymology, a 2,3-diaminopropionate N-oxalyltransferase () is an enzyme that catalyzes the chemical reaction
oxalyl-CoA + L-2,3-diaminopropanoate CoA + N3-oxalyl-L-2,3-diaminopropanoate
Thus, the two substrates of this enzyme are oxalyl-CoA and L-2,3-diaminopropanoate, whereas its two products are CoA and N3-oxalyl-L-2,3-diaminopropanoate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is oxalyl-CoA:L-2,3-diaminopropanoate N3-oxalyltransferase. Other names in common use include oxalyldiaminopropionate synthase, ODAP synthase, oxalyl-CoA:L-alpha,beta-diaminopropionic acid oxalyltransferase, oxalyldiaminopropionic synthase, and oxalyl-CoA:L-2,3-diaminopropanoate 3-N-oxalyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-acylglycerol-3-phosphate%20O-acyltransferase | In enzymology, a 2-acylglycerol-3-phosphate O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate CoA + 1,2-diacyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are acyl-CoA and 2-acyl-sn-glycerol 3-phosphate, whereas its two products are CoA and 1,2-diacyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase. This enzyme is also called 2-acylglycerophosphate acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-acylglycerol%20O-acyltransferase | In enzymology, a 2-acylglycerol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 2-acylglycerol CoA + diacylglycerol
Thus, the two substrates of this enzyme are acyl-CoA and 2-acylglycerol, whereas its two products are CoA and diacylglycerol.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:2-acylglycerol O-acyltransferase. Other names in common use include acylglycerol palmitoyltransferase, monoglyceride acyltransferase, acyl coenzyme A-monoglyceride acyltransferase, and monoacylglycerol acyltransferase. This enzyme participates in glycerolipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-acylglycerophosphocholine%20O-acyltransferase | In enzymology, a 2-acylglycerophosphocholine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine CoA + phosphatidylcholine
Thus, the two substrates of this enzyme are acyl-CoA and 2-acyl-sn-glycero-3-phosphocholine, whereas its two products are CoA and phosphatidylcholine.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:2-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Other names in common use include 2-acylglycerol-3-phosphorylcholine acyltransferase, and 2-acylglycerophosphocholine acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2alpha-hydroxytaxane%202-O-benzoyltransferase | In enzymology, a 2alpha-hydroxytaxane 2-O-benzoyltransferase () is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III CoA + 10-deacetylbaccatin III
Thus, the two substrates of this enzyme are benzoyl-CoA and 10-deacetyl-2-debenzoylbaccatin III, whereas its two products are CoA and 10-deacetylbaccatin III.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is benzoyl-CoA:taxan-2alpha-ol O-benzoyltransferase. This enzyme is also called benzoyl-CoA:taxane 2alpha-O-benzoyltransferase. This enzyme participates in diterpenoid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-ethylmalate%20synthase | In enzymology, a 2-ethylmalate synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + H2O + 2-oxobutanoate (R)-2-ethylmalate + CoA
The 3 substrates of this enzyme are acetyl-CoA, H2O, and 2-oxobutanoate, whereas its two products are (R)-2-ethylmalate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating), 2-ethylmalate-3-hydroxybutanedioate synthase, propylmalate synthase, and propylmalic synthase. This enzyme participates in pyruvate metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-hydroxyglutarate%20synthase | In enzymology, a 2-hydroxyglutarate synthase () is an enzyme that catalyzes the chemical reaction
propanoyl-CoA + H2O + glyoxylate 2-hydroxyglutarate + CoA
The 3 substrates of this enzyme are propanoyl-CoA, H2O, and glyoxylate, whereas its two products are 2-hydroxyglutarate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is propanoyl-CoA:glyoxylate C-propanoyltransferase (thioester-hydrolysing, 2-carboxyethyl-forming). Other names in common use include 2-hydroxyglutaratic synthetase, 2-hydroxyglutaric synthetase, alpha-hydroxyglutarate synthase, hydroxyglutarate synthase, and 2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating). This enzyme participates in c5-branched dibasic acid metabolism.
See also
D2HGDH
L2HGDH
2-hydroxyglutarate dehydrogenase
2-Hydroxyglutaric aciduria
Hydroxyacid-oxoacid transhydrogenase
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/2-isopropylmalate%20synthase | In enzymology, a 2-isopropylmalate synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 3-methyl-2-oxobutanoate + H2O (2S)-2-isopropylmalate + CoA
The three substrates of this enzyme are acetyl-CoA, 3-methyl-2-oxobutanoate, and H2O, and its products are (2S)-2-isopropylmalate and CoA.
The enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming). Other names in common use include 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase, (CoA-acetylating), alpha-isopropylmalate synthetase, alpha-isopropylmalate synthase, alpha-isopropylmalic synthetase, isopropylmalate synthase, and isopropylmalate synthetase. This enzyme participates in biosynthesis of L-leucine and pyruvate metabolism. Monovalent and divalent cation activation have been reported for enzymes from different sources.
Mycobacterium tuberculosis α-isopropylmalate synthase requires a divalent metal ion, of which Mg2+ and Mn2+ give highest activity, and a monovalent cation, with K+ as the best activator. Zn2+ was shown to be an inhibitor, contrary to what was assumed from the structural data. Another feature of the M. tuberculosis homolog is that L-leucine, the feedback inhibitor, inhibits the enzyme in a time-dependent fashion. This was the first demon |
https://en.wikipedia.org/wiki/2-methylcitrate%20synthase | In enzymology, a 2-methylcitrate synthase () is an enzyme that catalyzes the chemical reaction
propanoyl-CoA + H2O + oxaloacetate (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
The 3 substrates of this enzyme are propanoyl-CoA, H2O, and oxaloacetate, whereas its two products are (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming). Other names in common use include 2-methylcitrate oxaloacetate-lyase, MCS, methylcitrate synthase, and methylcitrate synthetase. This enzyme participates in propanoate metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3%2C4-dichloroaniline%20N-malonyltransferase | In enzymology, a 3,4-dichloroaniline N-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + 3,4-dichloroaniline CoA + N-(3,4-dichlorophenyl)-malonamate
Thus, the two substrates of this enzyme are malonyl-CoA and 3,4-dichloroaniline, whereas its two products are CoA and N-(3,4-dichlorophenyl)-malonamate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:3,4-dichloroaniline N-malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-ethylmalate%20synthase | In enzymology, a 3-ethylmalate synthase () is an enzyme that catalyzes the chemical reaction
butanoyl-CoA + H2O + glyoxylate 3-ethylmalate + CoA
The 3 substrates of this enzyme are butanoyl-CoA, H2O, and glyoxylate, whereas its two products are 3-ethylmalate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is butanoyl-CoA:glyoxylate C-butanoyltransferase (thioester-hydrolysing, 1-carboxypropyl-forming). Other names in common use include 2-ethyl-3-hydroxybutanedioate synthase, and 3-ethylmalate glyoxylate-lyase (CoA-butanoylating). This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Norman%E2%80%93Roberts%20syndrome | Norman–Roberts syndrome is a rare form of microlissencephaly caused by a mutation in the RELN gene. A small number of cases have been described. The syndrome was first reported by Margaret Grace Norman and M. Roberts et al. in 1976.
Lack of reelin prevents normal layering of the cerebral cortex and disrupts cognitive development. Patients have cerebellar hypoplasia, congenital lymphedema, and hypotonia. The disorder is also associated with myopia, nystagmus and generalized seizures.
Norman–Roberts syndrome is one of two known disorders caused by a disruption of the reelin-signaling pathway. The other is VLDLR-associated cerebellar hypoplasia, which is caused by a mutation in the gene coding for one of the reelin receptors, VLDLR.
Disruption of the RELN gene in human patients is analogous to the malfunctioning RELN gene in the reeler mouse.
References
External links
Description at US NIH Library of Medicine site
Congenital disorders
Neurological disorders
Rare syndromes |
https://en.wikipedia.org/wiki/3-oxoadipyl-CoA%20thiolase | In enzymology, a 3-oxoadipyl-CoA thiolase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + acetyl-CoA CoA + 3-oxoadipyl-CoA
Thus, the two substrates of this enzyme are succinyl-CoA and acetyl-CoA, whereas its two products are CoA and 3-oxoadipyl-CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is succinyl-CoA:acetyl-CoA C-succinyltransferase. This enzyme participates in benzoate degradation via hydroxylation.
3-Oxoadipyl-CoA thiolase belongs to the thiolase family of enzymes.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/3-propylmalate%20synthase | In enzymology, a 3-propylmalate synthase () is an enzyme that catalyzes the chemical reaction
pentanoyl-CoA + H2O + glyoxylate 3-propylmalate + CoA
The 3 substrates of this enzyme are pentanoyl-CoA, H2O, and glyoxylate, whereas its two products are 3-propylmalate and CoA.
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is pentanoyl-CoA:glyoxylate C-pentanoyltransferase (thioester-hydrolysing, 1-carboxybutyl-forming). Other names in common use include 3-(n-propyl)-malate synthase, 3-propylmalate glyoxylate-lyase (CoA-pentanoylating), beta-n-propylmalate synthase, and n-propylmalate synthase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/6%27-Deoxychalcone%20synthase | In enzymology, a 6'-deoxychalcone synthase () is an enzyme that catalyzes the chemical reaction
3 malonyl-CoA + 4-coumaroyl-CoA + NADPH + H+ 4 CoA + isoliquiritigenin + 3 CO2 + NADP+ + H2O
The 4 substrates of this enzyme are malonyl-CoA, 4-coumaroyl-CoA, NADPH, and H+, whereas its 5 products are CoA, isoliquiritigenin, CO2, NADP+, and H2O. Deoxychalcone synthase catalyzed activity is involved in the biosynthesis of retrochalcone and certain phytoalexins in the cells of Glycyrrhiza echinata (Russian licorice) and other leguminous plants.
This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is malonyl-CoA:4-coumaroyl-CoA malonyltransferase (cyclizing, reducing).
References
EC 2.3.1
NADPH-dependent enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/8-amino-7-oxononanoate%20synthase | In enzymology, a 8-amino-7-oxononanoate synthase () is an enzyme that catalyzes the chemical reaction
6-carboxyhexanoyl-CoA + L-alanine 8-amino-7-oxononanoate + CoA + CO2
Thus, the two substrates of this enzyme are 6-carboxyhexanoyl-CoA and L-alanine, whereas its 3 products are 8-amino-7-oxononanoate, CoA, and CO2.
This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
Nomenclature
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is 6-carboxyhexanoyl-CoA:L-alanine C-carboxyhexanoyltransferase (decarboxylating). Other names in common use include 7-keto-8-aminopelargonic acid synthetase, 7-keto-8-aminopelargonic synthetase, and 8-amino-7-oxopelargonate synthase.
References
Further reading
EC 2.3.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Acetyl-CoA%20C-acetyltransferase | In enzymology, an acetyl-CoA C-acetyltransferase () is an enzyme that catalyzes the chemical reaction
2 acetyl-CoA CoA + acetoacetyl-CoA
Hence, this enzyme has one substrate, acetyl-CoA, and two products, CoA and acetoacetyl-CoA.
Acetyl-CoA C-acetyltransferase belongs to the thiolase family of enzymes.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:acetyl-CoA C-acetyltransferase. Other names in common use include acetoacetyl-CoA thiolase, beta-acetoacetyl coenzyme A thiolase, 2-methylacetoacetyl-CoA thiolase [misleading], 3-oxothiolase, acetyl coenzyme A thiolase, acetyl-CoA acetyltransferase, acetyl-CoA:N-acetyltransferase, and thiolase II. This enzyme participates in 10 metabolic pathways: fatty acid metabolism, synthesis and degradation of ketone bodies, valine, leucine and isoleucine degradation, lysine degradation, tryptophan metabolism, pyruvate metabolism, benzoate degradation via coa ligation, propanoate metabolism, butanoate metabolism, and two-component system - general.
Isozymes
Human genes encoding acetyl-CoA C-acetyltransferases include:
References
Further reading
EC 2.3.1
Enzymes of known structure |
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