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https://en.wikipedia.org/wiki/Acetyl-CoA%20C-myristoyltransferase | In enzymology, an acetyl-CoA C-myristoyltransferase () is an enzyme that catalyzes the chemical reaction
myristoyl-CoA + acetyl-CoA 3-oxopalmitoyl-CoA + CoA
Thus, the two substrates of this enzyme are myristoyl-CoA and acetyl-CoA, whereas its two products are 3-oxopalmitoyl-CoA and 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 myristoyl-CoA:acetyl-CoA C-myristoyltransferase.
References
External links
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acridone%20synthase | In enzymology, an acridone synthase () is an enzyme that catalyzes the chemical reaction
3 malonyl-CoA + N-methylanthraniloyl-CoA 4 CoA + 1,3-dihydroxy-N-methylacridone + 3 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and N-methylanthraniloyl-CoA, whereas its 3 products are CoA, 1,3-dihydroxy-N-methylacridone, and CO2.
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:N-methylanthraniloyl-CoA malonyltransferase (cyclizing). This enzyme participates in acridone alkaloid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-%28acyl-carrier-protein%29%E2%80%94phospholipid%20O-acyltransferase | In enzymology, an acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3-phospho)ethanolamine [acyl-carrier protein] + O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine
Thus, the two substrates of this enzyme are acyl-acyl-carrier protein and O-(2-acyl-sn-glycero-3-phospho)ethanolamine, whereas its two products are acyl-carrier protein and O-(1,2-diacyl-sn-glycero-3-phospho)ethanolamine.
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-[acyl-carrier protein]:O-(2-acyl-sn-glycero-3-phospho)ethanolamine O-acyltransferase. Other names in common use include acyl-[acyl-carrier, protein]:O-(2-acyl-sn-glycero-3-phospho)-ethanolamine, and O-acyltransferase. This enzyme participates in glycerophospholipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Acyl-%28acyl-carrier-protein%29%E2%80%94UDP-N-acetylglucosamine%20O-acyltransferase | In enzymology, an acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase () is an enzyme that catalyzes the chemical reaction
(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetylglucosamine [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
Thus, the two substrates of this enzyme are (R)-3-hydroxytetradecanoyl-acyl-carrier-protein and UDP-N-acetylglucosamine, whereas its two products are acyl-carrier-protein and UDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine.
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 (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl) transferase. Other names in common use include UDP-N-acetylglucosamine acyltransferase and uridine diphosphoacetylglucosamine acyltransferase. This enzyme participates in lipopolysaccharide biosynthesis.
Structural studies
As of late 2007, 7 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/%28acyl-carrier-protein%29%20S-acetyltransferase | In enzymology, a [acyl-carrier-protein] S-acetyltransferase () is an enzyme that catalyzes the reversible chemical reaction
acetyl-CoA + [acyl-carrier-protein] CoA + acetyl-[acyl-carrier-protein]
Thus, the two substrates of this enzyme are acetyl-CoA and acyl carrier protein, whereas its two products are CoA and acetyl-acyl-carrier-protein.
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:[acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, Acetyl CoA:ACP transacylase, [acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/%28acyl-carrier-protein%29%20S-malonyltransferase | In enzymology, a [acyl-carrier-protein] S-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + acyl carrier protein CoA + malonyl-[acyl-carrier-protein]
Thus, the two substrates of this enzyme are malonyl-CoA and acyl carrier protein, whereas its two products are CoA and malonyl-acyl-carrier-protein. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in fatty acid biosynthesis.
Nomenclature
The systematic name of this enzyme class is malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase. Other names in common use include malonyl coenzyme A-acyl carrier protein transacylase,
[acyl carrier protein]malonyltransferase,
FabD,
malonyl transacylase,
malonyl transferase,
malonyl-CoA-acyl carrier protein transacylase,
malonyl-CoA:ACP transacylase,
malonyl-CoA:AcpM transacylase,
malonyl-CoA:acyl carrier protein transacylase,
MAT, and
MCAT.
Structure
Crystal Structures of FabD from E.coli and Streptomyces coelicolor are known and provide great insight into the catalytic mechanism of FabD. In E.Coli, FabD primarily involved in FAS pathway. However, in Streptomyces coelicolor, FabD is involved in FAS and polyketide synthase pathways. In both cases, the structures and active sites are very similar.
The protein has an α/β type architecture, but the fold is unique. the active site inferred from the location of the cat |
https://en.wikipedia.org/wiki/Agaritine%20gamma-glutamyltransferase | In enzymology, an agaritine gamma-glutamyltransferase () is an enzyme that catalyzes the chemical reaction
agaritine + acceptor 4-hydroxymethylphenylhydrazine + gamma-L-glutamyl-acceptor
Thus, the two substrates of this enzyme are agaritine and acceptor, whereas its two products are 4-hydroxymethylphenylhydrazine and gamma-L-glutamyl-acceptor.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is (gamma-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:acceptor gamma-glutamyltransferase. Other names in common use include (gamma-L-glutamyl)-N1-(4-hydroxymethylphenyl)hydrazine:(acceptor), gamma-glutamyltransferase, (gamma-L-glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:(acceptor), gamma-glutamyltransferase, (gamma-L-glutamyl)-1-N-(4-hydroxymethylphenyl)hydrazine:acceptor, and gamma-glutamyltransferase.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Agmatine%20N4-coumaroyltransferase | In enzymology, an agmatine N4-coumaroyltransferase () is an enzyme that catalyzes the chemical reaction
4-coumaroyl-CoA + agmatine CoA + N-(4-guanidinobutyl)-4-hydroxycinnamamide
Thus, the two substrates of this enzyme are 4-coumaroyl-CoA and agmatine, whereas its two products are CoA and N-(4-guanidinobutyl)-4-hydroxycinnamamide.
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 4-coumaroyl-CoA:agmatine N4-coumaroyltransferase. Other names in common use include p-coumaroyl-CoA-agmatine N-p-coumaroyltransferase, agmatine coumaroyltransferase, and 4-coumaroyl-CoA:agmatine 4-N-coumaroyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alanylphosphatidylglycerol%20synthase | In enzymology, an alanylphosphatidylglycerol synthase () is an enzyme that catalyzes the chemical reaction
L-alanyl-tRNA + phosphatidylglycerol tRNA + 3-O-L-alanyl-1-O-phosphatidylglycerol
Thus, the two substrates of this enzyme are L-alanyl-tRNA and phosphatidylglycerol, whereas its two products are tRNA and 3-O-L-alanyl-1-O-phosphatidylglycerol.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-alanyl-tRNA:phosphatidylglycerol alanyltransferase. Other names in common use include O-alanylphosphatidylglycerol synthase, and alanyl phosphatidylglycerol synthetase.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alcohol%20O-acetyltransferase | In enzymology, an alcohol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an alcohol CoA + an acetyl ester
Thus, the two substrates of this enzyme are acetyl-CoA and alcohol, whereas its two products are CoA and an acetyl ester.
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:alcohol O-acetyltransferase. This enzyme is also called alcohol acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alcohol%20O-cinnamoyltransferase | In enzymology, an alcohol O-cinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
1-O-trans-cinnamoyl-beta-D-glucopyranose + ROH alkyl cinnamate + glucose
Thus, the two substrates of this enzyme are 1-O-trans-cinnamoyl-beta-D-glucopyranose and an alkanol (ROH), whereas its two products are alkyl cinnamate and glucose.
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 1-O-trans-cinnamoyl-beta-D-glucopyranose:alcohol O-cinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alkylglycerophosphate%202-O-acetyltransferase | In enzymology, an alkylglycerophosphate 2-O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + 1-alkyl-sn-glycero-3-phosphate CoA + 1-alkyl-2-acetyl-sn-glycero-3-phosphate
Thus, the two substrates of this enzyme are acetyl-CoA and 1-alkyl-sn-glycero-3-phosphate, whereas its two products are CoA and 1-alkyl-2-acetyl-sn-glycero-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 acetyl-CoA:1-alkyl-sn-glycero-3-phosphate 2-O-acetyltransferase. This enzyme is also called alkyllyso-GP:acetyl-CoA acetyltransferase. This enzyme participates in ether lipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Alpha-tubulin%20N-acetyltransferase | In enzymology, an alpha-tubulin N-acetyltransferase () is an enzyme which is encoded by the ATAT1 gene.
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:[alpha-tubulin]-L-lysine N6-acetyltransferase. Other names in common use include alpha-tubulin acetylase, αTAT, ATAT1, TAT, alpha-TAT, alpha-tubulin acetyltransferase, tubulin N-acetyltransferase, acetyl-CoA:alpha-tubulin-L-lysine N-acetyltransferase, and acetyl-CoA:[alpha-tubulin]-L-lysine 6-N-acetyltransferase.
Structure
Primary
This protein has a length of 421 amino acids, among which, we have to highlight the Glutamine number 58 (Gln or Q), which is crucial for catalytic activity.
Secondary
ATAT1 has 8 α-helix, 10 β-strands and one turn. However, only half of the protein has a defined secondary conformation. The rest of this protein is intrinsically disordered.
Domains
ATAT1 it is not a modular protein because it only have one domain localized from the first amino acid to the one hundred and ninety.
Regions
It must be highlighted two important regions of ATAT1 (124-137 and 160-269), because is here where junction points with Acetyl-coA are.
Recently, studies describing the crystal structure of ATAT1 suggest that residues 196 to 236 of human ATAT1 (where acetylated lysines K210 and K221 are located) are disordered and do not contribute significantly to catalytic activity. |
https://en.wikipedia.org/wiki/Aminoglycoside%20N3%27-acetyltransferase | In enzymology, an aminoglycoside N3'-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + a 2-deoxystreptamine antibiotic CoA + N3'-acetyl-2-deoxystreptamine antibiotic
Thus, the two substrates of this enzyme are acetyl-CoA and 2-deoxystreptamine antibiotic, whereas its two products are CoA and N3'-acetyl-2-deoxystreptamine antibiotic.
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:2-deoxystreptamine-antibiotic N3'-acetyltransferase. Other names in common use include 3'-aminoglycoside acetyltransferase, and 3-N-aminoglycoside acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aminoglycoside%20N6%27-acetyltransferase | In enzymology, an aminoglycoside N6'-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + kanamycin-B CoA + N6'-acetylkanamycin-B
Thus, the two substrates of this enzyme are acetyl-CoA and kanamycin B, whereas its two products are CoA and N6'-acetylkanamycin-B.
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:kanamycin-B N6'-acetyltransferase. Other names in common use include aminoglycoside 6'-N-acetyltransferase, aminoglycoside-6'-acetyltransferase, aminoglycoside-6-N-acetyltransferase, and kanamycin acetyltransferase.
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/Anthocyanin%205-aromatic%20acyltransferase | In enzymology, an anthocyanin 5-aromatic acyltransferase () is an enzyme that catalyzes the chemical reaction
hydroxycinnamoyl-CoA + anthocyanidin-3,5-diglucoside CoA + anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside
Thus, the two substrates of this enzyme are hydroxycinnamoyl-CoA and anthocyanidin-3,5-diglucoside, whereas its two products are CoA and anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside.
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 hydroxycinnamoyl-CoA:anthocyanidin 3,5-diglucoside 5-O-glucoside-6"'-O-hydroxycinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure
Anthocyanins metabolism |
https://en.wikipedia.org/wiki/Anthocyanin%205-O-glucoside%206%27%27%27-O-malonyltransferase | In enzymology, an anthocyanin 5-O-glucoside 6'''-O-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside CoA + 4'''-demalonylsalvianin
Thus, the two substrates of this enzyme are malonyl-CoA and pelargonidin 3-O-(6-caffeoyl-beta-D-glucoside) 5-O-beta-D-glucoside, whereas its two products are CoA and 4'''-demalonylsalvianin.
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:pelargonidin-3-O-(6-caffeoyl-beta-D-glucoside)-5-O-beta- D-glucoside 6'''-O-malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthocyanin%206%22-O-malonyltransferase | In enzymology, an anthocyanin 6"-O-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + an anthocyanidin 3-O-beta-D-glucoside CoA + an anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside)
Thus, the two substrates of this enzyme are malonyl-CoA and anthocyanidin 3-O-beta-D-glucoside, whereas its two products are CoA and anthocyanidin 3-O-(6-O-malonyl-beta-D-glucoside).
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:anthocyanidin-3-O-beta-D-glucoside 6"-O-malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Anthranilate%20N-benzoyltransferase | In enzymology, an anthranilate N-benzoyltransferase () is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + anthranilate CoA + N-benzoylanthranilate
Thus, the two substrates of this enzyme are benzoyl-CoA and anthranilate, whereas its two products are CoA and N-benzoylanthranilate.
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:anthranilate N-benzoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure
Anthranilates |
https://en.wikipedia.org/wiki/Anthranilate%20N-malonyltransferase | In enzymology, an anthranilate N-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + anthranilate CoA + N-malonylanthranilate
Thus, the two substrates of this enzyme are malonyl-CoA and anthranilate, whereas its two products are CoA and N-malonylanthranilate.
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:anthranilate N-malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arginine%20N-succinyltransferase | In enzymology, an arginine N-succinyltransferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + L-arginine CoA + N2-succinyl-L-arginine
Thus, the two substrates of this enzyme are succinyl-CoA and L-arginine, whereas its two products are CoA and N2-succinyl-L-arginine.
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:L-arginine N2-succinyltransferase. Other names in common use include arginine succinyltransferase, AstA, arginine and ornithine N2-succinyltransferase, AOST, AST, and succinyl-CoA:L-arginine 2-N-succinyltransferase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
Further reading
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Arginyltransferase | In enzymology, an arginyltransferase () is an enzyme that catalyzes the chemical reaction
L-arginyl-tRNA + protein tRNA + L-arginyl-protein
Thus, the two substrates of this enzyme are L-arginyl-tRNA and protein, whereas its two products are tRNA and L-arginyl-protein.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-arginyl-tRNA:protein arginyltransferase. Other names in common use include arginine transferase, arginyl-transfer ribonucleate-protein aminoacyltransferase, arginyl-transfer ribonucleate-protein transferase, and arginyl-tRNA protein transferase. It has 2 cofactors: mercaptoethanol, and Cation.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aromatic-hydroxylamine%20O-acetyltransferase | In enzymology, an aromatic-hydroxylamine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl
Thus, the two substrates of this enzyme are N-hydroxy-4-acetylaminobiphenyl and N-hydroxy-4-aminobiphenyl, whereas its two products are N-hydroxy-4-aminobiphenyl and N-acetoxy-4-aminobiphenyl.
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 N-hydroxy-4-acetylaminobiphenyl:N-hydroxy-4-aminobiphenyl O-acetyltransferase. Other names in common use include aromatic hydroxylamine acetyltransferase, arylhydroxamate acyltransferase, arylhydroxamate N,O-acetyltransferase, arylhydroxamic acid N,O-acetyltransferase, arylhydroxamic acyltransferase, N,O-acetyltransferase, and N-hydroxy-2-acetylaminofluorene N-O acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Arylamine%20N-acetyltransferase | In enzymology, an arylamine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an arylamine CoA + an N-acetylarylamine
Thus, the two substrates of this enzyme are acetyl-CoA and arylamine, whereas its two products are CoA and N-acetylarylamine.
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:arylamine N-acetyltransferase. Other names in common use include arylamine acetylase, beta-naphthylamine N-acetyltransferase, 4-aminobiphenyl N-acetyltransferase, acetyl CoA-arylamine N-acetyltransferase, 2-naphthylamine N-acetyltransferase, arylamine acetyltransferase, indoleamine N-acetyltransferase, N-acetyltransferase, p-aminosalicylate N-acetyltransferase, serotonin acetyltransferase, and serotonin N-acetyltransferase.
Structural studies
As of late 2007, 7 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/Aspartate%20N-acetyltransferase | In enzymology, an aspartate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-aspartate CoA + N-acetyl-L-aspartate
Thus, the two substrates of this enzyme are acetyl-CoA and L-aspartate, whereas its two products are CoA and N-acetyl-L-aspartate.
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:L-aspartate N-acetyltransferase. Other names in common use include aspartate acetyltransferase, and L-aspartate N-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aspartyltransferase | In enzymology, an aspartyltransferase () is an enzyme that catalyzes the chemical reaction
L-asparagine + hydroxylamine NH3 + L-aspartylhydroxamate
Thus, the two substrates of this enzyme are L-asparagine and hydroxylamine, whereas its two products are NH3 and L-aspartylhydroxamate.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-asparagine:hydroxylamine gamma-aspartyltransferase. Other names in common use include beta-aspartyl transferase, and aspartotransferase.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ATP%20citrate%20synthase | ATP citrate synthase (also ATP citrate lyase (ACLY)) is an enzyme that in animals represents an important step in fatty acid biosynthesis. By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty acid biosynthesis, which consumes acetyl-CoA. In plants, ATP citrate lyase generates cytosolic acetyl-CoA precursors of thousands of specialized metabolites, including waxes, sterols, and polyketides.
Function
ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The enzyme is a tetramer of apparently identical subunits. In animals, the product, acetyl-CoA, is used in several important biosynthetic pathways, including lipogenesis and cholesterogenesis. It is activated by insulin.
In plants, ATP citrate lyase generates acetyl-CoA for cytosolically-synthesized metabolites; Acetyl-CoA is not transported across subcellular membranes of plants. Such metabolites include: elongated fatty acids (used in seed oils, membrane phospholipids, the ceramide moieties of sphingolipids, cuticle, cutin, and suberin); flavonoids; malonic acid; acetylated phenolics, alkaloids, isoprenoids, anthocyanins, and sugars; and, mevalonate-derived isoprenoids (e.g., sesquiterpenes, sterols, brassinosteroids); malonyl and acyl-derivatives (d-amino acids, malonylated flavonoids, acylated, prenylated and malonated proteins). De novo fatty acid biosynthesis in plants occurs in plastids |
https://en.wikipedia.org/wiki/Benzophenone%20synthase | In enzymology, a benzophenone synthase () is an enzyme that catalyzes the chemical reaction
3 malonyl-CoA + 3-hydroxybenzoyl-CoA 4 CoA + 2,3',4,6-tetrahydroxybenzophenone + 3 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and 3-hydroxybenzoyl-CoA, whereas its 3 products are CoA, 2,3',4,6-tetrahydroxybenzophenone, and CO2.
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-hydroxybenzoyl-CoA malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-glucogallin%20O-galloyltransferase | In enzymology, a beta-glucogallin O-galloyltransferase () is an enzyme that catalyzes the chemical reaction
2 1-O-galloyl-beta-D-glucose D-glucose + 1-O,6-O-digalloyl-beta-D-glucose
Hence, this enzyme has one substrate, 1-O-galloyl-beta-D-glucose, and two products, D-glucose and 1-O,6-O-digalloyl-beta-D-glucose.
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 1-O-galloyl-beta-D-glucose:1-O-galloyl-beta-D-glucose O-galloyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-glucogallin%E2%80%94tetrakisgalloylglucose%20O-galloyltransferase | In enzymology, a beta-glucogallin-tetrakisgalloylglucose O-galloyltransferase () is an enzyme that catalyzes the chemical reaction.
1-O-galloyl-beta-D-glucose + 1,2,3,6-tetrakis-O-galloyl-beta-D-glucose D-glucose + 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose
Thus, the two substrates of this enzyme are 1-O-galloyl-beta-D-glucose and 1,2,3,6-tetrakis-O-galloyl-beta-D-glucose, whereas its two products are D-glucose and 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose.
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 1-O-galloyl-beta-D-glucose:1,2,3,6-tetrakis-O-galloyl-beta-D-glucose 4-O-galloyltransferase. Other names in common use include beta-glucogallin-tetragalloylglucose 4-galloyltransferase, beta-glucogallin:1,2,3,6-tetra-O-galloylglucose, 4-O-galloyltransferase, beta-glucogallin:1,2,3,6-tetra-O-galloyl-beta-D-glucose, and 4-O-galloyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-ketoacyl-ACP%20synthase%20I | In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase I () is an enzyme that catalyzes the chemical reaction
an acyl-acyl-carrier-protein + malonyl-acyl-carrier-protein a 3-oxoacyl-acyl-carrier-protein + CO2 + acyl-carrier-protein
Thus, the two substrates of this enzyme are acyl-acyl-carrier-protein and malonyl-acyl-carrier-protein, whereas its 3 products are 3-oxoacyl-acyl-carrier-protein, CO2, and acyl carrier protein. This enzyme participates in fatty acid biosynthesis.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups.
Nomenclature
The systematic name of this enzyme class is acyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-protein] C-acyltransferase (decarboxylating).
Other names in common use include:
beta-ketoacyl-ACP synthase I,
beta-ketoacyl synthetase,
beta-ketoacyl-ACP synthetase,
beta-ketoacyl-acyl carrier protein synthetase,
beta-ketoacyl-[acyl carrier protein] synthase,
beta-ketoacylsynthase,
condensing enzyme (CE),
3-ketoacyl-acyl carrier protein synthase,
fatty acid condensing enzyme,
acyl-malonyl(acyl-carrier-protein)-condensing enzyme,
acyl-malonyl acyl carrier protein-condensing enzyme,
beta-ketoacyl acyl carrier protein synthase,
3-oxoacyl-[acyl-carrier-protein] synthase,
3-oxoacyl:ACP synthase I,
KASI,
KAS I,
FabF1, and
FabB.
References
Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2 |
https://en.wikipedia.org/wiki/Beta-ketoacyl-ACP%20synthase%20II | In enzymology, a beta-ketoacyl-acyl-carrier-protein synthase II () is an enzyme that catalyzes the chemical reaction
(Z)-hexadec-11-enoyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]
Thus, the two substrates of this enzyme are (Z)-hexadec-11-enoyl-[acyl-carrier-protein] and malonyl-[acyl-carrier-protein], whereas its 3 products are (Z)-3-oxooctadec-13-enoyl-[acyl-carrier-protein], CO2, and acyl-carrier-protein.
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 (Z)-hexadec-11-enoyl-[acyl-carrier-protein]:malonyl-[acyl-carrier-pr otein] C-acyltransferase (decarboxylating). Other names in common use include KASII, KAS II, FabF, 3-oxoacyl-acyl carrier protein synthase I, and beta-ketoacyl-ACP synthase II. This enzyme participates in fatty acid biosynthesis.
References
Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd ed., vol. 1, ASM Press, Washington, DC, 1996, p. 612-636.
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Beta-ketoacyl-ACP%20synthase%20III | In enzymology, a β-ketoacyl-[acyl-carrier-protein] synthase III () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + malonyl-[acyl carrier protein] acetoacetyl-[acyl carrier protein] + CoA + CO2
Thus, the two substrates of this enzyme are acetyl-CoA and malonyl-[acyl-carrier-protein], whereas its 3 products are acetoacetyl-[acyl-carrier-protein], CoA, and CO2. This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups.
This enzyme participates in fatty acid biosynthesis. β-Ketoacyl-acyl-carrier-protein synthase III is involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The role of FabH in fatty acid synthesis has been described in Streptomyces glaucescens, Streptococcus pneumoniae, and Streptomyces coelicolor.
Nomenclature
The systematic name of this enzyme class is acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase. Other names in common use include:
Role in tuberculosis
Mycobacterium tuberculosis, the cause of tuberculosis, evades effective immune clearance through encapsulation, especially with mycolic acids that are particularly resistant to the normal degradative processes of macrophages. Furthermore, this capsule inhibits entry of antibiotics. The enzymes involved in mycolate biosynthesis are essential for survival and pathogenesis, and thus represent excellent drug targets.
In M. tuberculosis, the beta-ke |
https://en.wikipedia.org/wiki/Bile%20acid-CoA%3Aamino%20acid%20N-acyltransferase | In enzymology, a bile acid-CoA:amino acid N-acyltransferase () is an enzyme that catalyzes the chemical reaction
choloyl-CoA + glycine CoA + glycocholate
Thus, the two substrates of this enzyme are choloyl-CoA and glycine, whereas its two products are CoA and glycocholate.
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 choloyl-CoA:glycine N-choloyltransferase. Other names in common use include glycine-taurine N-acyltransferase, amino acid N-choloyltransferase, BAT, glycine N-choloyltransferase, BACAT, cholyl-CoA glycine-taurine N-acyltransferase, and cholyl-CoA:taurine N-acyltransferase. This enzyme participates in bile acid biosynthesis and taurine and hypotaurine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Biphenyl%20synthase | In enzymology, a biphenyl synthase () is an enzyme that catalyzes the chemical reaction:
3 malonyl-CoA + benzoyl-CoA 4 CoA + 3,5-dihydroxybiphenyl + 4 CO2
Thus, the two substrates of this enzyme are malonyl-CoA and benzoyl-CoA, whereas its three products are CoA, 3,5-dihydroxybiphenyl, and CO2.
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:benzoyl-CoA malonyltransferase. This enzyme is also called BIS.
References
EC 2.3.1 |
https://en.wikipedia.org/wiki/Carnitine%20O-acetyltransferase | Carnitine O-acetyltransferase also called carnitine acetyltransferase (CRAT, or CAT) () is an enzyme that encoded by the CRAT gene that catalyzes the chemical reaction
acetyl-CoA + carnitine CoA + acetylcarnitine
where the acetyl group displaces the hydrogen atom in the central hydroxyl group of carnitine.
Thus, the two substrates of this enzyme are acetyl-CoA and carnitine, whereas its two products are CoA and O-acetylcarnitine. The reaction is highly reversible and does not depend on the order in which substrates bind.
Different subcellular localizations of the CRAT mRNAs are thought to result from alternative splicing of the CRAT gene suggested by the divergent sequences in the 5' region of peroxisomal and mitochondrial CRAT cDNAs and the location of an intron where the sequences diverge. The alternatively splicing of this gene results in three distinct isoforms, one of which contains an N-terminal mitochondrial transit peptide, and has been shown to be located in mitochondria.
Nomenclature
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 acetyl-CoA:carnitine O-acetyltransferase. Other names in common use include acetyl-CoA-carnitine O-acetyltransferase, acetylcarnitine transferase, carnitine acetyl coenzyme A transferase, carnitine acetylase, carnitine acetyltransferase, carnitine-acetyl-CoA transferase, and CATC. This enzyme par |
https://en.wikipedia.org/wiki/Carnitine%20O-octanoyltransferase | Carnitine O-octanoyltransferase (CROT or COT) is a member of the transferase family, more specifically a carnitine acyltransferase, a type of enzyme which catalyzes the transfer of acyl groups from acyl-CoAs to carnitine, generating CoA and an acyl-carnitine. () The systematic name of this enzyme is octanoyl-CoA:L-carnitine O-octanoyltransferase. Other names in common use include medium-chain/long-chain carnitine acyltransferase, carnitine medium-chain acyltransferase, easily solubilized mitochondrial carnitine palmitoyltransferase, and overt mitochondrial carnitine palmitoyltransferase. Specifically, CROT catalyzes the chemical reaction:
octanoyl-CoA + L-carnitine CoA + L-octanoylcarnitine
Thus, the two substrates of this enzyme are octanoyl-CoA and L-carnitine and its two products are CoA and L-octanoylcarnitine.
This reaction is easily chemically reversible, and does not require any energy input, as both fatty acyl-CoAs and fatty acylcarnitines are considered chemically “activated” forms of fatty acyl groups.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups.
Structure
CROT is 612 amino acids long, with a molecular weight of about 70 kDa. In terms of broad overall structural features, CROT has 20 α-helices and 16 β-strands, and can be divided into two overall domains, named N and C.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , |
https://en.wikipedia.org/wiki/CDP-acylglycerol%20O-arachidonoyltransferase | In enzymology, a CDP-acylglycerol O-arachidonoyltransferase () was an enzyme construed to catalyze the chemical reaction
arachidonoyl-CoA + CDP-acylglycerol CoA + CDP-diacylglycerol
When discovered in 1979, the two substrates of this enzyme were believed to be arachidonoyl-CoA and CDP-acylglycerol, whereas its two products were CoA and CDP-diacylglycerol.
Such enzyme were describes as transferases, specifically acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class was arachidonoyl-CoA:CDP-acylglycerol O-arachidonoyltransferase. Other names also found are CDP-acylglycerol O-arachidonyltransferase, and arachidonyl-CoA:CDP-acylglycerol O-arachidonyltransferase. Such enzyme was presumably participating in glycerophospholipid metabolism.
However, no CDP-acylglycerol O-arachidonoyltransferase has been characterized, the reaction demonstrated in 1979 by Thompson and MacDonald was not reproducible. In 1983, W. Thomson retracted his discovery explaining possible contamination of their batch of liponucleotides.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chlorogenate%E2%80%94glucarate%20O-hydroxycinnamoyltransferase | In enzymology, a chlorogenate-glucarate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
chlorogenate + glucarate quinate + 2-O-caffeoylglucarate
Thus, the two substrates of this enzyme are chlorogenate and glucarate, whereas its two products are quinate and 2-O-caffeoylglucarate.
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 chlorogenate:glucarate O-(hydroxycinnamoyl)transferase. Other names in common use include chlorogenate:glucarate caffeoyltransferase, chlorogenic acid:glucaric acid O-caffeoyltransferase, and chlorogenate:glucarate caffeoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Citrate%20%28Re%29-synthase | In enzymology, a citrate (Re)-synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + H2O + oxaloacetate citrate + CoA
The 3 substrates of this enzyme are acetyl-CoA, H2O, and oxaloacetate, whereas its two products are citrate 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:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-R)-carboxymethyl-forming]. Other names in common use include (R)-citrate synthase, Re-citrate-synthase, and citrate oxaloacetate-lyase [(pro-3R)-CH2COO-->acetyl-CoA].
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cortisol%20O-acetyltransferase | In enzymology, a cortisol O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + cortisol CoA + cortisol 21-acetate
Thus, the two substrates of this enzyme are acetyl-CoA and cortisol, whereas its two products are CoA and cortisol 21-acetate.
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:cortisol O-acetyltransferase. Other names in common use include cortisol acetyltransferase, corticosteroid acetyltransferase, and corticosteroid-21-O-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cysteine-S-conjugate%20N-acetyltransferase | In enzymology, a cysteine-S-conjugate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an S-substituted L-cysteine CoA + an S-substituted N-acetyl-L-cysteine
Thus, the two substrates of this enzyme are acetyl-CoA and S-substituted L-cysteine, whereas its two products are CoA and S-substituted N-acetyl-L-cysteine.
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:S-substituted L-cysteine N-acetyltransferase. This enzyme participates in glutathione metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-alanine%20gamma-glutamyltransferase | In enzymology, a D-alanine gamma-glutamyltransferase () is an enzyme that catalyzes the chemical reaction
L-glutamine + D-alanine NH3 + gamma-L-glutamyl-D-alanine
Thus, the two substrates of this enzyme are L-glutamine and D-alanine, whereas its two products are NH3 and gamma-L-glutamyl-D-alanine.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-glutamine:D-alanine gamma-glutamyltransferase.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/ZPR | ZPR May refer to:
Xánica Zapotec, ISO 639-3 language code zpr
Preston Road tube station, London, England, National Rail station code ZPR
The LITTLE ZIPPER (ZPR) protein, the first microprotein discovered in plants
ZPR Media Group, a media company in Poland
Zero power reactors, identifier of several research nuclear reactors at Argonne National Laboratory; see List of nuclear research reactors#United States |
https://en.wikipedia.org/wiki/D-amino-acid%20N-acetyltransferase | In enzymology, a D-amino-acid N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + a D-amino acid CoA + an N-acetyl-D-amino acid
Thus, the two substrates of this enzyme are acetyl-CoA and D-amino acid, whereas its two products are CoA and N-acetyl-D-amino acid.
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:D-amino-acid N-acetyltransferase. Other names in common use include D-amino acid acetyltransferase, and D-amino acid-alpha-N-acetyltransferase. This enzyme participates in phenylalanine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetylcephalosporin-C%20acetyltransferase | In enzymology, a deacetylcephalosporin-C acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + deacetylcephalosporin C CoA + cephalosporin C
Thus, the two substrates of this enzyme are acetyl-CoA and deacetylcephalosporin C, whereas its two products are CoA and cephalosporin 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:deacetylcephalosporin-C O-acetyltransferase. Other names in common use include acetyl-CoA:deacetylcephalosporin-C acetyltransferase, DAC acetyltransferase, cefG, deacetylcephalosporin C acetyltransferase, acetyl coenzyme A:DAC acetyltransferase, acetyl-CoA:DAC acetyltransferase, CPC acetylhydrolase, acetyl-CoA:DAC O-acetyltransferase, and DAC-AT. This enzyme participates in penicillin and cephalosporin biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetyl-%28citrate-%28pro-3S%29-lyase%29%20S-acetyltransferase | In enzymology, a deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase () is an enzyme that catalyzes the chemical reaction
S-acetylphosphopantetheine + deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)] phosphopantetheine + [citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)]
Thus, the two substrates of this enzyme are S-acetylphosphopantetheine and [[deacetyl-[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)]]], whereas its two products are phosphopantetheine and [[citrate-oxaloacetate-lyase((pro-3S)-CH2COO-->acetate)]].
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 S-acetylphosphopantetheine:deacetyl-[citrate-oxaloacetate-lyase((pro -3S)-CH2COO-->acetate)] S-acetyltransferase. Other names in common use include S-acetyl phosphopantetheine:deacetyl citrate lyase, S-acetyltransferase, and deacetyl-[citrate-(pro-3S)-lyase] acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Deacetylvindoline%20O-acetyltransferase | In enzymology, a deacetylvindoline O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + deacetylvindoline CoA + vindoline
Thus, the two substrates of this enzyme are acetyl-CoA and deacetylvindoline, whereas its two products are CoA and vindoline.
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:deacetylvindoline 4-O-acetyltransferase. Other names in common use include deacetylvindoline acetyltransferase, DAT, 17-O-deacetylvindoline-17-O-acetyltransferase, acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase, acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase, acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase, acetylcoenzyme A:deacetylvindoline O-acetyltransferase, 17-O-deacetylvindoline O-acetyltransferase, and acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase. This enzyme participates in terpene indole and ipecac alkaloid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Decylcitrate%20synthase | Decylcitrate synthase () is an enzyme that catalyzes the chemical reaction in enzymology.
lauroyl-CoA + H2O + oxaloacetate (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate + CoA
The 3 substrates of this enzyme are lauroyl-CoA, H2O, and oxaloacetate, whereas its two products are (2S,3S)-2-hydroxytridecane-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 dodecanoyl-CoA:oxaloacetate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming). Other names in common use include 2-decylcitrate synthase, (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase, and (CoA-acylating).
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Decylhomocitrate%20synthase | In enzymology, a decylhomocitrate synthase () is an enzyme that catalyzes the chemical reaction
dodecanoyl-CoA + H2O + 2-oxoglutarate (3S,4S)-3-hydroxytetradecane-1,3,4-tricarboxylate + CoA
The 3 substrates of this enzyme are dodecanoyl-CoA, H2O, and 2-oxoglutarate, whereas its two products are (3S,4S)-3-hydroxytetradecane-1,3,4-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 dodecanoyl-CoA:2-oxoglutarate C-dodecanoyltransferase (thioester-hydrolysing, 1-carboxyundecyl-forming). Other names in common use include 2-decylhomocitrate synthase, 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase, and (CoA-acylating).
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-glutamyltransferase | In enzymology, a D-glutamyltransferase () is an enzyme that catalyzes the chemical reaction
L(or D)-glutamine + D-glutamyl-peptide NH3 + 5-glutamyl-D-glutamyl-peptide
The 3 substrates of this enzyme are L-glutamine, D-glutamine, and D-glutamyl-peptide, whereas its two products are NH3 and 5-glutamyl-D-glutamyl-peptide.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is glutamine:D-glutamyl-peptide 5-glutamyltransferase. Other names in common use include D-glutamyl transpeptidase, and D-gamma-glutamyl transpeptidase. This enzyme participates in d-glutamine and d-glutamate metabolism.
References
EC 2.3.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diacylglycerol%E2%80%94sterol%20O-acyltransferase | In enzymology, a diacylglycerol-sterol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
1,2-diacyl-sn-glycerol + sterol monoacylglycerol + sterol ester
Thus, the two substrates of this enzyme are 1,2-diacyl-sn-glycerol and sterol, whereas its two products are monoacylglycerol and sterol ester.
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 1,2-diacyl-sn-glycerol:sterol O-acyltransferase. This enzyme is also called 1,2-diacyl-sn-glycerol:sterol acyl transferase. This enzyme participates in bile acid biosynthesis.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diamine%20N-acetyltransferase | In enzymology, a diamine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + an alkane-alpha,omega-diamine CoA + an N-acetyldiamine
Thus, the two substrates of this enzyme are acetyl-CoA and alkane-alpha,omega-diamine, whereas its two products are CoA and N-acetyldiamine.
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:alkane-alpha,omega-diamine N-acetyltransferase. Other names in common use include spermidine acetyltransferase, putrescine acetyltransferase, putrescine (diamine)-acetylating enzyme, diamine acetyltransferase, spermidine/spermine N1-acetyltransferase, spermidine N1-acetyltransferase, acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase, putrescine acetylase, and putrescine N-acetyltransferase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies
As of late 2007, 12 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/Diaminobutyrate%20acetyltransferase | In enzymology, a diaminobutyrate acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-2,4-diaminobutanoate CoA + N4-acetyl-L-2,4-diaminobutanoate
Thus, the two substrates of this enzyme are acetyl-CoA and L-2,4-diaminobutanoate, whereas its two products are CoA and N4-acetyl-L-2,4-diaminobutanoate.
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:L-2,4-diaminobutanoate N4-acetyltransferase. Other names in common use include L-2,4-diaminobutyrate acetyltransferase, L-2,4-diaminobutanoate acetyltransferase, EctA, diaminobutyric acid acetyltransferase, DABA acetyltransferase, 2,4-diaminobutanoate acetyltransferase, DAB acetyltransferase, DABAcT, and acetyl-CoA:L-2,4-diaminobutanoate 4-N-acetyltransferase. This enzyme participates in glycine, serine and threonine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue%20%282-methylpropanoyl%29transferase | In enzymology, a dihydrolipoyllysine-residue (2-methylpropanoyl)transferase () is an enzyme that catalyzes the chemical reaction
2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine
Thus, the two substrates of this enzyme are 2-methylpropanoyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and [[enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine]].
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 2-methylpropanoyl-CoA:enzyme-N6-(dihydrolipoyl)lysine S-(2-methylpropanoyl)transferase. Other names in common use include dihydrolipoyl transacylase, enzyme-dihydrolipoyllysine:2-methylpropanoyl-CoA, S-(2-methylpropanoyl)transferase, 2-methylpropanoyl-CoA:enzyme-6-N-(dihydrolipoyl)lysine, and S-(2-methylpropanoyl)transferase. This enzyme participates in valine, leucine and isoleucine degradation.
Structural studies
As of late 2007, 6 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/Dihydrolipoyllysine-residue%20succinyltransferase | In enzymology, a dihydrolipoyllysine-residue succinyltransferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
Thus, the two substrates of this enzyme are succinyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and enzyme N6-(S-succinyldihydrolipoyl)lysine.
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:enzyme-N6-(dihydrolipoyl)lysine S-succinyltransferase. Other names in common use include dihydrolipoamide S-succinyltransferase, dihydrolipoamide succinyltransferase, dihydrolipoic transsuccinylase, dihydrolipolyl transsuccinylase, dihydrolipoyl transsuccinylase, lipoate succinyltransferase (Escherichia coli), lipoic transsuccinylase, lipoyl transsuccinylase, succinyl-CoA:dihydrolipoamide S-succinyltransferase, succinyl-CoA:dihydrolipoate S-succinyltransferase, and enzyme-dihydrolipoyllysine:succinyl-CoA S-succinyltransferase. This enzyme participates in citrate cycle (tca cycle) and lysine degradation.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
References
Boyer, P.D. (Ed.), The Enzymes, 3rd ed., vol. 1, Academic Press, New York, 1970, p. 213-240.
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dolichol%20O-acyltransferase | In enzymology, a dolichol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
palmitoyl-CoA + dolichol CoA + dolichyl palmitate
Thus, the two substrates of this enzyme are palmitoyl-CoA and dolichol, whereas its two products are CoA and dolichyl palmitate.
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 palmitoyl-CoA:dolichol O-palmitoyltransferase. This enzyme is also called acyl-CoA:dolichol acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-tryptophan%20N-acetyltransferase | In enzymology, a D-tryptophan N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + D-tryptophan CoA + N-acetyl-D-tryptophan
Thus, the two substrates of this enzyme are acetyl-CoA and D-tryptophan, whereas its two products are CoA and N-acetyl-D-tryptophan.
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:D-tryptophan N-acetyltransferase. Other names in common use include D-tryptophan acetyltransferase, and acetyl-CoA-D-tryptophan-alpha-N-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-tryptophan%20N-malonyltransferase | In enzymology, a D-tryptophan N-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + D-tryptophan CoA + N2-malonyl-D-tryptophan
Thus, the two substrates of this enzyme are malonyl-CoA and D-tryptophan, whereas its two products are CoA and N2-malonyl-D-tryptophan.
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:D-tryptophan N-malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ecdysone%20O-acyltransferase | In enzymology, an ecdysone O-acyltransferase () is an enzyme that catalyzes the chemical reaction
palmitoyl-CoA + ecdysone CoA + ecdysone palmitate
Thus, the two substrates of this enzyme are palmitoyl-CoA and ecdysone, whereas its two products are CoA and ecdysone palmitate.
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 palmitoyl-CoA:ecdysone palmitoyltransferase. Other names in common use include acyl-CoA:ecdysone acyltransferase, and fatty acyl-CoA:ecdysone acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Erythronolide%20synthase | In enzymology, an erythronolide synthase (also 6-Deoxyerythronolide B Synthase or DEBS) is an enzyme that catalyzes the chemical reaction
6 malonyl-CoA + propanoyl-CoA 7 CoA + 6-deoxyerythronolide B
Thus, the two substrates of this enzyme are malonyl-CoA and propanoyl-CoA, whereas its two products are CoA and 6-deoxyerythronolide b. This enzyme participates in biosynthesis of 12-, 14- and 16-membered macrolides.
This enzyme belongs to the family of transferases, it has been identified as part of a Type 1 polyketide synthase module. DEBS is found in Saccharopolyspora erythraea and other actinobacteria, and is responsible for the synthesis of the macrolide ring which is the precursor of the antibiotic erythromycin. There have been three categories of polyketide synthases identified to date, type 1, 2 and 3. Type one synthases involve large multidomain proteins containing all the sites necessary for polyketide synthesis. Type two synthases contain active sites distributed among several smaller polypeptides, and type three synthases are large multi-protein complexes containing modules which have a single active site for each and every step of polyketide synthesis. In the case of DEBS, there are three large multi-functional proteins, DEBS 1,2, and 3, that each exist as a dimer of two modules. Each module consists of a minimum of a Ketosynthase (KS), Acyl carrier protein (ACP) site, and acyltransferase (AT), but may also contain a Ketoreductase (KR), Dehydrotase (DH), and E |
https://en.wikipedia.org/wiki/Fatty-acyl-CoA%20synthase | Fatty-acyl-CoA Synthase, or more commonly known as yeast fatty acid synthase (and not to be confused with Long Chain fatty acyl-CoA synthetase), is an enzyme complex responsible for fatty acid biosynthesis, and is of Type I Fatty Acid Synthesis (FAS). Yeast fatty acid synthase plays a pivotal role in fatty acid synthesis. It is a 2.6 MDa barrel shaped complex and is composed of two, unique multi-functional subunits: alpha and beta. Together, the alpha and beta units are arranged in an α6β6 structure. The catalytic activities of this enzyme complex involves a coordination system of enzymatic reactions between the alpha and beta subunits. The enzyme complex therefore consists of six functional centers for fatty acid synthesis.
Reaction
The enzyme catalyzes the reaction:
Acetyl-CoA + n malonyl-CoA + 4n NADPH + 4n H+ long-chain-acyl-CoA + n CoA + n CO2 + 4n NADP+
The 4 substrates of this enzyme are acetyl-CoA, malonyl-CoA, NADPH, and H+, whereas its 4 products are Acyl-CoA, CoA, CO2, and NADP+.
More specifically, the FAS catalysis mechanism consumes an acetyl-coenzyme A (acetyl-CoA) and seven malonyl-CoA molecules to produce a Palmitoyl-CoA.
Background
Synthesis of fatty acids is generally performed by fatty acid synthase (FAS). Though the syntheses of fatty acids are very similar across all organisms, the enzymes and subsequent enzymatic mechanisms involved in fatty acid synthesis vary between eukaryotes and prokaryotes. There are two types of fatty acid synthesis (FAS |
https://en.wikipedia.org/wiki/Flavonol-3-O-beta-glucoside%20O-malonyltransferase | In enzymology, a flavonol-3-O-beta-glucoside O-malonyltransferase () is an enzyme that catalyzes the chemical reaction
malonyl-CoA + flavonol 3-O-beta-D-glucoside CoA + flavonol 3-O-(6-O-malonyl-beta-D-glucoside)
Thus, the two substrates of this enzyme are malonyl-CoA and flavonol 3-O-beta-D-glucoside, whereas its two products are CoA and flavonol 3-O-(6-O-malonyl-beta-D-glucoside).
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:flavonol-3-O-beta-D-glucoside 6"-O-malonyltransferase. Other names in common use include flavonol 3-O-glucoside malonyltransferase, MAT-3, and malonyl-coenzyme A:flavonol-3-O-glucoside malonyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Flavonol-3-O-triglucoside%20O-coumaroyltransferase | In enzymology, a flavonol-3-O-triglucoside O-coumaroyltransferase () is an enzyme that catalyzes the chemical reaction
4-coumaroyl-CoA + a flavonol 3-O-[beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside] CoA + a flavonol 3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)- beta-D-glucoside]
The 3 substrates of this enzyme are 4-coumaroyl-CoA, flavonol, and [[3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside]], whereas its 4 products are CoA, flavonol, [[3-O-[6-(4-coumaroyl)-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-]], and beta-D-glucoside].
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 4-coumaroyl-CoA:flavonol-3-O-[beta-D-glucosyl-(1->2)-beta-D-glucosid e] 6-O-4-coumaroyltransferase.
References
EC 2.3.1
Enzymes of unknown structure
Flavanols metabolism |
https://en.wikipedia.org/wiki/Formate%20C-acetyltransferase | In enzymology, formate C-acetyltransferase (pyruvate formate lyase) () is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows:
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:formate C-acetyltransferase. Other names in common use include pyruvate formate-lyase, pyruvic formate-lyase, and formate acetyltransferase. This enzyme participates in 3 metabolic pathways: pyruvate metabolism, propanoate metabolism, and butanoate metabolism.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
Pyruvate formate lyase is a homodimer made of 85 kDa, 759-residue subunits. It has a 10-stranded beta/alpha barrel motif into which is inserted a beta finger that contains major catalytic residues. The active site of the enzyme, elucidated by x-ray crystallography, holds three essential amino acids that perform catalysis (Gly734, Cys418, and Cys419), three major residues that hold the substrate pyruvate close by (Arg435, Arg176, and Ala272), and two flanking hydrophobic residues (Trp333 and Phe432).
Studies have found structura |
https://en.wikipedia.org/wiki/Formylmethanofuran%E2%80%94tetrahydromethanopterin%20N-formyltransferase | In enzymology, a formylmethanofuran-tetrahydromethanopterin N-formyltransferase () is an enzyme that catalyzes the chemical reaction
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
Thus, the two substrates of this enzyme are formylmethanofuran and 5,6,7,8-tetrahydromethanopterin, whereas its two products are methanofuran and 5-formyl-5,6,7,8-tetrahydromethanopterin.
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 formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase. Other names in common use include formylmethanofuran-tetrahydromethanopterin formyltransferase, formylmethanofuran:tetrahydromethanopterin formyltransferase, N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT), formyltransferase, FTR, formylmethanofuran:5,6,7,8-tetrahydromethanopterin, and N5-formyltransferase. This enzyme participates in folate biosynthesis.
Ftr from the thermophilic methanogen Methanopyrus kandleri (which has an optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The crystal structure of Ftr, determined to a reveals a homotetramer composed essentially of two dimers. Each subunit is subdivided into two tightly associated lobes both consisting of a predominant |
https://en.wikipedia.org/wiki/Galactarate%20O-hydroxycinnamoyltransferase | In enzymology, a galactarate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
feruloyl-CoA + galactarate CoA + O-feruloylgalactarate
Thus, the two substrates of this enzyme are feruloyl-CoA and galactarate, whereas its two products are CoA and O-feruloylgalactarate.
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 feruloyl-CoA:galactarate O-(hydroxycinnamoyl)transferase. This enzyme is also called galacturate hydroxycinnamoyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactolipid%20O-acyltransferase | In enzymology, a galactolipid O-acyltransferase () is an enzyme that catalyzes the chemical reaction
2 mono-beta-D-galactosyldiacylglycerol acylmono-beta-D-galactosyldiacylglycerol + mono-beta-D-galactosylacylglycerol
Hence, this enzyme has one substrate, mono-beta-D-galactosyldiacylglycerol, and two products, acylmono-beta-D-galactosyldiacylglycerol and mono-beta-D-galactosylacylglycerol.
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 mono-beta-D-galactosyldiacylglycerol:mono-beta-D-galactosyldiacylgly cerol acyltransferase. This enzyme is also called galactolipid:galactolipid acyltransferase. This enzyme participates in glycerolipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Galactosylacylglycerol%20O-acyltransferase | In enzymology, a galactosylacylglycerol O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-[acyl-carrier-protein] + sn-3-D-galactosyl-sn-2-acylglycerol [acyl-carrier-protein] + D-galactosyldiacylglycerol
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and sn-3-D-galactosyl-sn-2-acylglycerol, whereas its two products are acyl-carrier-protein and D-galactosyldiacylglycerol.
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-[acyl-carrier-protein]:D-galactosylacylglycerol O-acyltransferase. Other names in common use include acyl-acyl-carrier protein: lysomonogalactosyldiacylglycerol, acyltransferase, and acyl-ACP:lyso-MGDG acyltransferase. This enzyme participates in glycerolipid metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gamma-glutamylcyclotransferase | In enzymology, a gamma-glutamylcyclotransferase () is an enzyme that catalyzes the chemical reaction
(5-L-glutamyl)-L-amino acid 5-oxoproline + L-amino acid
Hence, this enzyme has one substrate, (5-L-glutamyl)-L-amino acid, and two products, 5-oxoproline and L-amino acid.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is (5-L-glutamyl)-L-amino-acid 5-glutamyltransferase (cyclizing). Other names in common use include gamma-glutamyl-amino acid cyclotransferase, gamma-L-glutamylcyclotransferase, and L-glutamic cyclase. This enzyme participates in glutathione metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Paulsson | Paulsson is a Swedish patronymic surname meaning "son of Paul", itself an English language derivative of the ancient Roman (pre-Christian) nomen Paulus, meaning "small". There are over 200 variants of the surname. Within Sweden, an alternate spelling is Pålsson, while the Icelandic is Pálsson, and the British Isles is Paulson. Paulsson is uncommon as a given name.
People with the surname include:
Erik Paulsson, billionaire businessman
Gunnar S. Paulsson, British historian
Haakon Paulsson, joint Earl of Orkney
Marcus Paulsson, ice hockey player
References
Swedish-language surnames
Surnames
Patronymic surnames
Surnames from given names |
https://en.wikipedia.org/wiki/Gentamicin%202%27-N-acetyltransferase | In enzymology, a gentamicin 2'-N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + gentamicin C1a CoA + N2'-acetylgentamicin C1a
Thus, the two substrates of this enzyme are acetyl-CoA and gentamicin C1a, whereas its two products are CoA and N2'-acetyl gentamicin C1a.
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:gentamicin-C1a N2'-acetyltransferase. Other names in common use include gentamicin acetyltransferase II, gentamicin 2'-N-acetyltransferase, and acetyl-CoA:gentamicin-C1a N2'-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gentamicin%203%27-N-acetyltransferase | In enzymology, a gentamicin 3'-N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + gentamicin C CoA + N3'-acetylgentamicin C
Thus, the two substrates of this enzyme are acetyl-CoA and gentamicin C, whereas its two products are CoA and N3'-acetylgentamicin 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:gentamicin-C N3'-acetyltransferase. Other names in common use include gentamicin acetyltransferase I, aminoglycoside acetyltransferase AAC(3)-1, gentamicin 3'-N-acetyltransferase, and acetyl-CoA:gentamicin-C N3'-acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucarate%20O-hydroxycinnamoyltransferase | In enzymology, a glucarate O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
sinapoyl-CoA + glucarate CoA + O-sinapoylglucarate
Thus, the two substrates of this enzyme are sinapoyl-CoA and glucarate, whereas its two products are CoA and O-sinapoylglucarate.
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 sinapoyl-CoA:glucarate O-(hydroxycinnamoyl)transferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucarolactone%20O-hydroxycinnamoyltransferase | In enzymology, a glucarolactone O-hydroxycinnamoyltransferase () is an enzyme that catalyzes the chemical reaction
sinapoyl-CoA + glucarolactone CoA + O-sinapoylglucarolactone
Thus, the two substrates of this enzyme are sinapoyl-CoA and glucarolactone, whereas its two products are CoA and O-sinapoylglucarolactone.
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 sinapoyl-CoA:glucarolactone O-(hydroxycinnamoyl)transferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosamine-1-phosphate%20N-acetyltransferase | In enzymology, a glucosamine-1-phosphate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + alpha-D-glucosamine 1-phosphate CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Thus, the two substrates of this enzyme are acetyl-CoA and alpha-D-glucosamine 1-phosphate, whereas its two products are CoA and N-acetyl-alpha-D-glucosamine 1-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 acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, 3 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/Glucosamine%20N-acetyltransferase | In enzymology, a glucosamine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + D-glucosamine CoA + N-acetyl-D-glucosamine
Thus, the two substrates of this enzyme are acetyl-CoA and D-glucosamine, whereas its two products are CoA and N-acetyl-D-glucosamine.
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:D-glucosamine N-acetyltransferase. Other names in common use include glucosamine acetylase, and glucosamine acetyltransferase. This enzyme participates in aminosugars metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosamine-phosphate%20N-acetyltransferase | In enzymology, glucosamine-phosphate N-acetyltransferase (GNA) () is an enzyme that catalyzes the transfer of an acetyl group from acetyl-CoA to the primary amine in glucosamide-6-phosphate, generating a free CoA and N-acetyl-D-glucosamine-6-phosphate.
This enzyme belongs to the family of transferases, a group of enzymes that transfers a very specific functional group, in this case acetyl, from a donor to a receptor. Specifically, this enzyme can be characterized as part of the acyltransferases family, since it involves the transfer of a general acyl group with a methyl as the substituent.
Nomenclature
The systematic name of this enzyme class is acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase. Other names in common use include phosphoglucosamine transacetylase, phosphoglucosamine acetylase, glucosamine-6-phosphate acetylase, D-glucosamine-6-P N-acetyltransferase, aminodeoxyglucosephosphate acetyltransferase, glucosamine 6-phosphate acetylase, glucosamine 6-phosphate N-acetyltransferase, N-acetylglucosamine-6-phosphate synthase, phosphoglucosamine N-acetylase, glucosamine-phosphate N-acetyltransferase, and glucosamine-6-phosphate N-acetyltransferase.
Function
This enzyme is part of the hexosamine biosynthesis pathway (HBP), which is one of the glucose processing pathways in the general metabolism. This pathway shares the initial two steps with glycolysis and diverges only a small portion of glucose flux from this more traditional glycolytic pathway. Therefore, i |
https://en.wikipedia.org/wiki/Glutamate%20N-acetyltransferase | In enzymology, a glutamate N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
N2-acetyl-L-ornithine + L-glutamate L-ornithine + N-acetyl-L-glutamate
Thus, the two substrates of this enzyme are N2-acetyl-L-ornithine and L-glutamate, whereas its two products are L-ornithine and N-acetyl-L-glutamate.
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 N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase. Other names in common use include ornithine transacetylase, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, acetylglutamate synthetase, acetylglutamate-acetylornithine transacetylase, acetylglutamic synthetase, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, glutamate acetyltransferase, N-acetyl-L-glutamate synthetase, N-acetylglutamate synthase, N-acetylglutamate synthetase, ornithine acetyltransferase, and 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. This enzyme participates in urea cycle and metabolism of amino groups.
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/Alabandite | Alabandite or alabandine is a rarely occurring manganese sulfide mineral. It crystallizes in the cubic crystal system with the chemical composition Mn2+S and develops commonly massive to granular aggregates, but rarely also cubic or octahedral crystals to 1 cm.
Etymology and History
Alabandite was first described in 1784 by Franz-Joseph Müller von Reichenstein. The mineral name is derived from its supposed discovery locality at Alabanda (Aïdin) in Turkey.
Occurrence
Alabandite forms in epithermal polymetallic sulfide veins and low-temperature manganese deposits. It occurs with acanthite, calcite, chalcopyrite, galena, pyrite, quartz, rhodochrosite, rhodonite, sphalerite and native tellurium. Sometimes it was found in meteorites.
Localities are several areas in Antarctica, Argentina, Armenia, Australia, Bolivia, Brazil, Bulgaria, Canada, China, Czech Republic, Finland, France, Germany, Ghana, Greece, Greenland, India, Italy, Japan, Kyrgyzstan, Mexico, New Zealand, Norway, Peru, Poland, Romania, Russia, Slovakia, South Africa, South Korea, Sweden, Switzerland, Taiwan, Tanzania, the United Kingdom, the US, Uzbekistan and Yemen. All together at present time approximately 220 discovery sites are registered.
Crystal structure
Alabandite crystallizes in the cubic crystal system in the space group Fm3m with the lattice parameter a = 5.22 Å and four formula units per unit cell.
See also
List of minerals
References
Manganese(II) minerals
Sulfide minerals
Galena group
Cubic |
https://en.wikipedia.org/wiki/Glutamine%20N-acyltransferase | In enzymology, a glutamine N-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + L-glutamine CoA + N-acyl-L-glutamine
Thus, the two substrates of this enzyme are acyl-CoA and L-glutamine, whereas its two products are CoA and N-acyl-L-glutamine.
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:L-glutamine N-acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutamine%20N-phenylacetyltransferase | In enzymology, a glutamine N-phenylacetyltransferase () is an enzyme that catalyzes the chemical reaction
phenylacetyl-CoA + L-glutamine CoA + alpha-N-phenylacetyl-L-glutamine
Thus, the two substrates of this enzyme are phenylacetyl-CoA and L-glutamine, whereas its two products are CoA and alpha-N-phenylacetyl-L-glutamine.
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 phenylacetyl-CoA:L-glutamine alpha-N-phenylacetyltransferase. Other names in common use include glutamine phenylacetyltransferase, and phenylacetyl-CoA:L-glutamine N-acetyltransferase. This enzyme participates in tyrosine metabolism and phenylalanine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/0-2-4 | Under the Whyte notation for the classification of steam locomotives, 0-2-4 represents the wheel arrangement of no leading wheels, two powered driving wheels on one axle, and four trailing wheels on two axles.
History
This is an unusual wheel arrangement, with the only known examples being three locomotives supplied to the Dundee and Newtyle Railway by J and C Carmichael of Dundee in 1833. These were still in operation in 1847, but may have been scrapped in 1849 when the line was converted to the standard gauge.
There was also the Bristol and Exter Railway Fairfield Steam Carriage, Built in 1848 for the Bristol and Exter Railway, Who used it on a Branch line before turning it into a 0-2-2.
References
2,0-2-4 |
https://en.wikipedia.org/wiki/CELSR1 | Cadherin EGF LAG seven-pass G-type receptor 1 also known as flamingo homolog 2 or cadherin family member 9 is a protein that in humans is encoded by the CELSR1 gene.
Function
The protein encoded by this gene is a member of the flamingo subfamily, part of the cadherin superfamily. The flamingo subfamily consists of nonclassic-type cadherins; a subpopulation that does not interact with catenins. The flamingo cadherins are located at the plasma membrane and have nine cadherin domains, seven epidermal growth factor-like repeats and two laminin G-like domains in their ectodomain. They also have seven transmembrane domains, a characteristic unique to this subfamily. It is postulated that these proteins are receptors involved in contact-mediated communication, with cadherin domains acting as homophilic binding regions and the EGF-like domains involved in cell adhesion and receptor-ligand interactions. This particular member is a developmentally regulated, neural-specific gene which plays an unspecified role in early embryogenesis.
See also
Flamingo (protein)
References
External links
Further reading
Adhesion G protein-coupled receptors
Chemokine receptors |
https://en.wikipedia.org/wiki/Glutaminyl-peptide%20cyclotransferase | In enzymology, a glutaminyl-peptide cyclotransferase () is an enzyme that catalyzes the chemical reaction
L-glutaminyl-peptide 5-oxoprolyl-peptide + NH3 or
L-glutamyl-peptide 5-oxoprolyl-peptide + H2O
Hence, this enzyme has one substrate, L-glutaminyl-peptide or L-glutamyl-peptide, and two products, 5-oxoprolyl-peptide and NH3 or H2O. The N-terminal 5-oxoproline residue on the peptide is also commonly known as pyroglutamic acid.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is L-glutaminyl-peptide gamma-glutamyltransferase (cyclizing). Other names in common use include glutaminyl-tRNA cyclotransferase, glutaminyl cyclase, and glutaminyl-transfer ribonucleate cyclotransferase.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , and .
Human gene
QPCT - note that Q is one-letter abbreviation for glutamine, and glutaminyl is the name of the acyl group.
References
EC 2.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutathione%20gamma-glutamylcysteinyltransferase | In enzymology, a glutathione gamma-glutamylcysteinyltransferase () is an enzyme that catalyzes the chemical reaction
glutathione + [Glu(-Cys)]n-Gly Gly + [Glu(-Cys)]n+1-Gly
Thus, the two substrates of this enzyme are glutathione and [Glu(-Cys)]n-Gly, whereas its two products are Gly and [Glu(-Cys)]n+1-Gly.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase. Other names in common use include phytochelatin synthase, and gamma-glutamylcysteine dipeptidyl transpeptidase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 2.3.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate%20O-acyltransferase | In enzymology, a glycerol-3-phosphate O-acyltransferase () is an enzyme that catalyzes the chemical reaction
acyl-CoA + sn-glycerol 3-phosphate CoA + 1-acyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are acyl-CoA and sn-glycerol 3-phosphate, whereas its two products are CoA and 1-acyl-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:sn-glycerol-3-phosphate 1-O-acyltransferase. Other names in common use include alpha-glycerophosphate acyltransferase, 3-glycerophosphate acyltransferase, ACP:sn-glycerol-3-phosphate acyltransferase, glycerol 3-phosphate acyltransferase, glycerol phosphate acyltransferase, glycerol phosphate transacylase, glycerophosphate acyltransferase, glycerophosphate transacylase, sn-glycerol 3-phosphate acyltransferase, and sn-glycerol-3-phosphate acyltransferase. This enzyme participates in glycerolipid metabolism and glycerophospholipid metabolism. The later pathways in human is part of the WikiPathways machine readable pathway collection.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and . Currently 4 different proteins are assigned to this reaction, GPAT1, GPAT2, GPAT3 and GPAT4. GPAT1 and 2 are considered mitochondrial proteins.
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycerophospholipid%20acyltransferase%20%28CoA-dependent%29 | In enzymology, a glycerophospholipid acyltransferase (CoA-dependent) () is an enzyme that catalyzes the chemical reaction
1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine
Thus, the two substrates of this enzyme are 1-organyl-2-acyl-sn-glycero-3-phosphocholine and 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine, whereas its two products are 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine and 1-organyl-2-lyso-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 1-organyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-gly cero-3-phosphoethanolamine acyltransferase (CoA-dependent).
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerophospholipid%20arachidonoyl-transferase%20%28CoA-independent%29 | In the field of enzymology, a glycerophospholipid arachidonoyl-transferase (CoA-independent) () is an enzyme that catalyzes the chemical reaction:
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine
This enzyme catalyzes the transfer of arachidonic acid and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso- glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups.
Nomenclature
The systematic name of this enzyme class is 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lys o-sn-glycero-3-phosphoethanolamine arachidonoyltransferase (CoA-independent).
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20C-acetyltransferase | In enzymology, a glycine C-acetyltransferase () is an enzyme that catalyzes the chemical reaction:
acetyl-CoA + glycine CoA + 2-amino-3-oxobutanoate
Thus, the two substrates of this enzyme are acetyl-CoA and glycine, whereas its two products are CoA and 2-amino-3-oxobutanoate.
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:glycine C-acetyltransferase. Other names in common use include 2-amino-3-ketobutyrate CoA ligase, 2-amino-3-ketobutyrate coenzyme A ligase, 2-amino-3-ketobutyrate-CoA ligase, glycine acetyltransferase, and aminoacetone synthase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
Human genes
GCAT
References
EC 2.3.1
Pyridoxal phosphate enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glycine%20N-acyltransferase | In enzymology, a glycine N-acyltransferase (GLYAT), also known as acyl-CoA:glycine N-acyltransferase (ACGNAT), () is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are acyl-CoA and glycine, whereas its two products are CoA and N-acylglycine. 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:glycine N-acyltransferase. Other names in common use include glycine acyltransferase, and glycine-N-acylase.
This enzyme plays a prominent role in converting benzoic acid (benzoate) into hippuric acid (N-benzoylglycine). Benzoic acid is metabolized by butyrate-CoA ligase into an intermediate product, benzoyl-CoA, which is then metabolized by glycine N-acyltransferase into hippuric acid.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycine%20N-benzoyltransferase | In enzymology, a glycine N-benzoyltransferase () is an enzyme that catalyzes the chemical reaction
benzoyl-CoA + glycine CoA + N-benzoylglycine
Thus, the two substrates of this enzyme are benzoyl-CoA and glycine, whereas its two products are CoA and N-benzoylglycine.
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:glycine N-benzoyltransferase. Other names in common use include benzoyl CoA-amino acid N-acyltransferase, and benzoyl-CoA:glycine N-acyltransferase. This enzyme participates in phenylalanine metabolism.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycoprotein%20N-palmitoyltransferase | In enzymology, a glycoprotein N-palmitoyltransferase () is an enzyme that catalyzes the chemical reaction
palmitoyl-CoA + glycoprotein CoA + N-palmitoylglycoprotein
Thus, the two substrates of this enzyme are palmitoyl-CoA and glycoprotein, whereas its two products are CoA and N-palmitoylglycoprotein.
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 palmitoyl-CoA:glycoprotein N-palmitoyltransferase. This enzyme is also called mucus glycoprotein fatty acyltransferase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, Dithiothreitol.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycoprotein%20O-fatty-acyltransferase | In enzymology, a glycoprotein O-fatty-acyltransferase () is an enzyme that catalyzes the chemical reaction
palmitoyl-CoA + mucus glycoprotein CoA + O-palmitoylglycoprotein
Thus, the two substrates of this enzyme are palmitoyl-CoA and mucus glycoprotein, whereas its two products are CoA and O-palmitoylglycoprotein.
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 fatty-acyl-CoA:mucus-glycoprotein fatty-acyltransferase. This enzyme is also called protein acyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycylpeptide%20N-tetradecanoyltransferase | In enzymology, a glycylpeptide N-tetradecanoyltransferase () is an enzyme that catalyzes the chemical reaction
tetradecanoyl-CoA + glycylpeptide CoA + N-tetradecanoylglycylpeptide
Thus, the two substrates of this enzyme are tetradecanoyl-CoA and glycylpeptide, whereas its two products are CoA and N-tetradecanoylglycylpeptide. It participates in the N-Myristoylation of proteins, and in vertebrates there are two isoenzymes NMT1 and NMT2.
Besides tetradecanoyl-CoA, this enzyme is also capable of using modified versions of this substrate. In human retina, an even wider range of fatty acids, including 14:1 n–9, 14:2n–6, and 12:0, are accepted by the enzyme and grafted onto guanylate cyclase activators. This is mainly a result of a special set of fatty-acid-CoA substrates available in the retina.
Nomenclature
This enzyme belongs to the family of transferases, specifically those N-acyltransferases transferring groups other than aminoacyl groups (cd04301). The systematic name of this enzyme class is tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase. Other names in common use include peptide N-myristoyltransferase (NMT), myristoyl-CoA-protein N-myristoyltransferase, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoylating enzymes, and protein N-myristoyltransferase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .
The enzyme folds into two domains, each with a double |
https://en.wikipedia.org/wiki/Histidine%20N-acetyltransferase | In enzymology, a histidine N-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-histidine CoA + N-acetyl-L-histidine
Thus, the two substrates of this enzyme are acetyl-CoA and L-histidine, whereas its two products are CoA and N-acetyl-L-histidine.
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:L-histidine N-acetyltransferase. Other names in common use include acetylhistidine synthetase, and histidine acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homocitrate%20synthase | In enzymology, a homocitrate synthase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + H2O + 2-oxoglutarate (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
The 3 substrates of this enzyme are acetyl-CoA, H2O, and 2-oxoglutarate, whereas its two products are (R)-2-hydroxybutane-1,2,4-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 acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming). Other names in common use include 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase, (CoA-acetylating), acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates in lysine biosynthesis and pyruvate metabolism.
References
EC 2.3.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Homoserine%20O-acetyltransferase | In enzymology, a homoserine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + L-homoserine CoA + O-acetyl-L-homoserine
Thus, the two substrates of this enzyme are acetyl-CoA and L-homoserine, whereas its two products are CoA and O-acetyl-L-homoserine.
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:L-homoserine O-acetyltransferase. Other names in common use include homoserine acetyltransferase, homoserine transacetylase, homoserine-O-transacetylase, and L-homoserine O-acetyltransferase. This enzyme participates in methionine metabolism and sulfur metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 2.3.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Homoserine%20O-succinyltransferase | In enzymology, a homoserine O-succinyltransferase () is an enzyme that catalyzes the chemical reaction
succinyl-CoA + L-homoserine CoA + O-succinyl-L-homoserine
Thus, the two substrates of this enzyme are succinyl-CoA and L-homoserine, whereas its two products are CoA and O-succinyl-L-homoserine.
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:L-homoserine O-succinyltransferase. Other names in common use include homoserine O-transsuccinylase, and homoserine succinyltransferase. This enzyme participates in methionine metabolism and sulfur metabolism.
Structural studies
As of late 2016, three 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/Hydrogen-sulfide%20S-acetyltransferase | In enzymology, a hydrogen-sulfide S-acetyltransferase () is an enzyme that catalyzes the chemical reaction
acetyl-CoA + hydrogen sulfide CoA + thioacetate
Thus, the two substrates of this enzyme are acetyl-CoA and hydrogen sulfide, whereas its two products are CoA and thioacetate.
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:hydrogen-sulfide S-acetyltransferase. This enzyme is also called hydrogen-sulfide acetyltransferase.
References
EC 2.3.1
Enzymes of unknown structure |
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