EC |
2.3.1.5 |
Accepted name: |
arylamine N-acetyltransferase |
Reaction: |
acetyl-CoA + an arylamine = CoA + an N-acetylarylamine |
Other name(s): |
arylamine acetylase; β-naphthylamine N-acetyltransferase; 4-aminobiphenyl N-acetyltransferase; acetyl CoA-arylamine N-acetyltransferase; 2-naphthylamine N-acetyltransferase; arylamine acetyltransferase; indoleamine N-acetyltransferase; N-acetyltransferase (ambiguous); p-aminosalicylate N-acetyltransferase; serotonin acetyltransferase; serotonin N-acetyltransferase |
Systematic name: |
acetyl-CoA:arylamine N-acetyltransferase |
Comments: |
Wide specificity for aromatic amines, including serotonin; also catalyses acetyl-transfer between arylamines without CoA. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-33-2 |
References: |
1. |
Chou, T.C. and Lipmann, F. Separation of acetyl transfer enzymes in pigeon liver extract. J. Biol. Chem. 196 (1952) 89–103. [PMID: 12980945] |
2. |
Paul, R.C. and Ratledge, C. Further studies on anthranilate N-acetylanthranilic acid in Aerobacter aerogenes. Biochim. Biophys. Acta 320 (1973) 9–15. [DOI] [PMID: 4748369] |
3. |
Tabor, H., Mehler, A.H. and Stadtman, E.R. The enzymatic acetylation of amines. J. Biol. Chem. 204 (1953) 127–138. [PMID: 13084583] |
4. |
Weissbach, H., Redfield, B.G. and Axelrod, J. The enzymic acetylation of serotonin and other naturally occurring amines. Biochim. Biophys. Acta 54 (1961) 190–192. [DOI] [PMID: 14005907] |
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[EC 2.3.1.5 created 1961] |
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EC |
2.3.1.50 |
Accepted name: |
serine C-palmitoyltransferase |
Reaction: |
palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 |
Other name(s): |
serine palmitoyltransferase; SPT; 3-oxosphinganine synthetase; acyl-CoA:serine C-2 acyltransferase decarboxylating |
Systematic name: |
palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating) |
Comments: |
A pyridoxal-phosphate protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-50-7 |
References: |
1. |
Brady, R.N., DiMari, S.J. and Snell, E.E. Biosynthesis of sphingolipid bases. 3. Isolation and characterization of ketonic intermediates in the synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri. J. Biol. Chem. 244 (1969) 491–496. [PMID: 4388074] |
2. |
Stoffel, W., Le Kim, D. and Sticht, G. Biosynthesis of dihydrosphingosine in vitro. Hoppe-Seyler's Z. Physiol. Chem. 349 (1968) 664–670. [PMID: 4386961] |
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[EC 2.3.1.50 created 1976, modified 1982] |
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EC |
2.3.1.51 |
Accepted name: |
1-acylglycerol-3-phosphate O-acyltransferase |
Reaction: |
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate |
Other name(s): |
1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase |
Systematic name: |
acyl-CoA:1-acyl-sn-glycerol-3-phosphate 2-O-acyltransferase |
Comments: |
Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51901-16-7 |
References: |
1. |
Frentzen, M., Heinz, E., McKeon, T.A. and Stumpf, P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629–636. [DOI] [PMID: 6825679] |
2. |
Hill, E.E. and Lands, W.E.M. Incorporation of long-chain and polyunsaturated acids into phosphatidate and phosphatidylcholine. Biochim. Biophys. Acta 152 (1968) 645–648. [DOI] [PMID: 5661029] |
3. |
Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123] |
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[EC 2.3.1.51 created 1976, modified 1990] |
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EC |
2.3.1.52 |
Accepted name: |
2-acylglycerol-3-phosphate O-acyltransferase |
Reaction: |
acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate |
Other name(s): |
2-acylglycerophosphate acyltransferase |
Systematic name: |
acyl-CoA:2-acyl-sn-glycerol 3-phosphate O-acyltransferase |
Comments: |
Saturated acyl-CoA thioesters are the most effective acyl donors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 51901-17-8 |
References: |
1. |
Yamashita, S., Hosaka, K. and Numa, S. Acyl-donor specificities of partially purified 1-acylglycerophosphate acyltransferase, 2-acylglycerophosphate acyltransferase and 1-acylglycerophosphorylcholine acyltransferase from rat-liver microsomes. Eur. J. Biochem. 38 (1973) 25–31. [DOI] [PMID: 4774123] |
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[EC 2.3.1.52 created 1976] |
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EC |
2.3.1.53 |
Accepted name: |
phenylalanine N-acetyltransferase |
Reaction: |
acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine |
Other name(s): |
acetyl-CoA-L-phenylalanine α-N-acetyltransferase |
Systematic name: |
acetyl-CoA:L-phenylalanine N-acetyltransferase |
Comments: |
Also acts, more slowly, on L-histidine and L-alanine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-16-5 |
References: |
1. |
Leuzinger, W., Baker, A.L. and Cauvin, E. Acetylcholinesterase. II. Crystallization, absorption spectra, isoionic point. Proc. Natl. Acad. Sci. USA 59 (1968) 620–623. [DOI] [PMID: 5238989] |
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[EC 2.3.1.53 created 1976] |
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EC |
2.3.1.54 |
Accepted name: |
formate C-acetyltransferase |
Reaction: |
acetyl-CoA + formate = CoA + pyruvate |
Other name(s): |
pyruvate formate-lyase; pyruvic formate-lyase; formate acetyltransferase |
Systematic name: |
acetyl-CoA:formate C-acetyltransferase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9068-08-0 |
References: |
1. |
Knappe, J., Blaschkowski, H.P., Grobner, P. and Schmitt, T. Pyruvate formate-lyase of Escherichia coli: the acetyl-enzyme intermediate. Eur. J. Biochem. 50 (1974) 253–263. [DOI] [PMID: 4615902] |
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[EC 2.3.1.54 created 1976] |
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EC
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2.3.1.55
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Deleted entry: | kanamycin 6′-N-acetyltransferase identical to EC 2.3.1.82 aminoglycoside N6′-acetyltransferase |
[EC 2.3.1.55 created 1976, deleted 1999] |
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EC |
2.3.1.56 |
Accepted name: |
aromatic-hydroxylamine O-acetyltransferase |
Reaction: |
N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl = N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl |
Other name(s): |
aromatic hydroxylamine acetyltransferase; arylhydroxamate acyltransferase; arylhydroxamate N,O-acetyltransferase; arylhydroxamic acid N,O-acetyltransferase; arylhydroxamic acyltransferase; N,O-acetyltransferase; N-hydroxy-2-acetylaminofluorene N-O acyltransferase |
Systematic name: |
N-hydroxy-4-acetylaminobiphenyl:N-hydroxy-4-aminobiphenyl O-acetyltransferase |
Comments: |
Transfers the N-acetyl group of some aromatic acethydroxamates to the O-position of some aromatic hydroxylamines. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52660-15-8 |
References: |
1. |
Bartsch, H., Dworkin, C., Miller, E.C. and Miller, J.A. Formation of electrophilic N-acetoxyarylamines in cytosoles from rat mammary gland and other tissues by transacetylation from the carcinogen N-hydroxy-4-acetylaminobiphenyl. Biochim. Biophys. Acta 304 (1973) 42–55. [DOI] [PMID: 4699998] |
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[EC 2.3.1.56 created 1976] |
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EC |
2.3.1.57 |
Accepted name: |
diamine N-acetyltransferase |
Reaction: |
acetyl-CoA + an alkane-α,ω-diamine = CoA + an N-acetyldiamine |
Glossary: |
spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine |
Other name(s): |
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; putrescine N-acetyltransferase |
Systematic name: |
acetyl-CoA:alkane-α,ω-diamine N-acetyltransferase |
Comments: |
Acts on propane-1,3-diamine, pentane-1,5-diamine, putrescine, spermidine (forming N1- and N8-acetylspermidine), spermine, N1-acetylspermidine and N8-acetylspermidine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 54596-36-0 |
References: |
1. |
Della Ragione, F. and Pegg, A.E. Purification and characterization of spermidine/spermine N1-acetyltransferase from rat liver. Biochemistry 21 (1982) 6152–6158. [PMID: 7150547] |
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[EC 2.3.1.57 created 1976, modified 1989] |
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EC |
2.3.1.58 |
Accepted name: |
2,3-diaminopropionate N-oxalyltransferase |
Reaction: |
oxalyl-CoA + L-2,3-diaminopropanoate = CoA + N3-oxalyl-L-2,3-diaminopropanoate |
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For diagram of O3-Acetyl-L-serine metabolism, click here |
Other name(s): |
oxalyldiaminopropionate synthase; ODAP synthase; oxalyl-CoA:L-α,β-diaminopropionic acid oxalyltransferase; oxalyldiaminopropionic synthase; oxalyl-CoA:L-2,3-diaminopropanoate 3-N-oxalyltransferase |
Systematic name: |
oxalyl-CoA:L-2,3-diaminopropanoate N3-oxalyltransferase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-48-3 |
References: |
1. |
Malathi, K., Padmanaban, G. and Sarma, P.S. Biosynthesis of β-N-oxalyl-L-α,β-diaminopropionic acid, the Lathyrus sativus neurotoxin. Phytochemistry 9 (1970) 1603–1610. |
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[EC 2.3.1.58 created 1976] |
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EC |
2.3.1.59 |
Accepted name: |
gentamicin 2′-N-acetyltransferase |
Reaction: |
acetyl-CoA + gentamicin C1a = CoA + N2′-acetylgentamicin C1a |
Glossary: |
kanamycin |
Other name(s): |
gentamycin acetyltransferase II; gentamycin 2′-N-acetyltransferase; acetyl-CoA:gentamycin-C1a N2′-acetyltransferase |
Systematic name: |
acetyl-CoA:gentamicin-C1a N2′-acetyltransferase |
Comments: |
The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, neomycin B, kanamycin B and kanamycin C can also act as acceptors. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 50864-40-9 |
References: |
1. |
Benveniste, R. and Davies, J. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc. Natl. Acad. Sci. USA 70 (1973) 2276–2280. [DOI] [PMID: 4209515] |
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[EC 2.3.1.59 created 1976] |
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