The Enzyme Database

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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, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, 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]
[EC 2.3.1.5 created 1961]
 
 
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, 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]
[EC 2.3.1.50 created 1976, modified 1982]
 
 
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, 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]
[EC 2.3.1.51 created 1976, modified 1990]
 
 
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]
[EC 2.3.1.52 created 1976]
 
 
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]
[EC 2.3.1.53 created 1976]
 
 
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]
[EC 2.3.1.54 created 1976]
 
 
EC 2.3.1.55      
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]
 
 
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]
[EC 2.3.1.56 created 1976]
 
 
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]
[EC 2.3.1.57 created 1976, modified 1989]
 
 
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
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.
[EC 2.3.1.58 created 1976]
 
 
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, 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]
[EC 2.3.1.59 created 1976]
 
 


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