The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 2.3.1.3     
Accepted name: glucosamine N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine
Other name(s): glucosamine acetylase; glucosamine acetyltransferase
Systematic name: acetyl-CoA:D-glucosamine N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9032-94-4
References:
1.  Chou, T.C. and Soodak, M. The acetylation of D-glucosamine by pigeon liver extracts. J. Biol. Chem. 196 (1952) 105–109. [PMID: 12980946]
[EC 2.3.1.3 created 1961]
 
 
EC 2.3.1.30     
Accepted name: serine O-acetyltransferase
Reaction: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
For diagram of O3-Acetyl-L-serine metabolism, click here
Glossary: O-acetyl-L-serine = (2S)-3-acetyloxy-2-aminopropanoic acid
Other name(s): SATase; L-serine acetyltransferase; serine acetyltransferase; serine transacetylase
Systematic name: acetyl-CoA:L-serine O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-16-9
References:
1.  Kredich, N.M. and Tomkins, G.M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241 (1966) 4955–4965. [PMID: 5332668]
2.  Smith, I.K. and Thompson, J.F. Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris). Biochim. Biophys. Acta 227 (1971) 288–295. [DOI] [PMID: 5550822]
[EC 2.3.1.30 created 1972]
 
 
EC 2.3.1.31     
Accepted name: homoserine O-acetyltransferase
Reaction: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Other name(s): homoserine acetyltransferase; homoserine transacetylase; homoserine-O-transacetylase; L-homoserine O-acetyltransferase
Systematic name: acetyl-CoA:L-homoserine O-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-72-2
References:
1.  Nagai, S. and Flavin, M. Acetylhomoserine. An intermediate in the fungal biosynthesis of methionine. J. Biol. Chem. 242 (1967) 3884–3895. [PMID: 6037552]
[EC 2.3.1.31 created 1972]
 
 
EC 2.3.1.32     
Accepted name: lysine N-acetyltransferase
Reaction: acetyl phosphate + L-lysine = phosphate + N6-acetyl-L-lysine
Other name(s): lysine acetyltransferase; acetyl-phosphate:L-lysine 6-N-acetyltransferase
Systematic name: acetyl-phosphate:L-lysine N6-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-12-8
References:
1.  Paik, W.K. and Kim, S. Enzymic synthesis of ε-N-acetyl-L-lysine. Arch. Biochem. Biophys. 108 (1964) 221–229. [DOI] [PMID: 14240571]
[EC 2.3.1.32 created 1972]
 
 
EC 2.3.1.33     
Accepted name: histidine N-acetyltransferase
Reaction: acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine
Other name(s): acetylhistidine synthetase; histidine acetyltransferase
Systematic name: acetyl-CoA:L-histidine N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-59-2
References:
1.  Baslow, M.H. N-acetyl-L-histidine synthetase activity from the brain of the killifish. Brain Res. 3 (1966) 210–213. [DOI] [PMID: 5971525]
[EC 2.3.1.33 created 1972]
 
 
EC 2.3.1.34     
Accepted name: D-tryptophan N-acetyltransferase
Reaction: acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan
Other name(s): D-tryptophan acetyltransferase; acetyl-CoA-D-tryptophan-α-N-acetyltransferase
Systematic name: acetyl-CoA:D-tryptophan N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-13-9
References:
1.  Zenk, M.H. and Schmitt, J. Enzymatische Acetylierung von D-Tryptophan. Naturwissenschaften 51 (1964) 510–511.
[EC 2.3.1.34 created 1972]
 
 
EC 2.3.1.35     
Accepted name: glutamate N-acetyltransferase
Reaction: N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate
Other name(s): ornithine transacetylase; α-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; 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase
Systematic name: N2-acetyl-L-ornithine:L-glutamate N-acetyltransferase
Comments: Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-14-0
References:
1.  Staub, M. and Dénes, G. Mechanism of arginine biosynthesis in Chlamydomonas reinhardti. I. Purification and properties of ornithine acetyltransferase. Biochim. Biophys. Acta 128 (1966) 82–91. [PMID: 5972370]
[EC 2.3.1.35 created 1972]
 
 
EC 2.3.1.36     
Accepted name: D-amino-acid N-acetyltransferase
Reaction: acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid
Other name(s): D-amino acid acetyltransferase; D-amino acid-α-N-acetyltransferase
Systematic name: acetyl-CoA:D-amino-acid N-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-15-1
References:
1.  Zenk, M.H. and Schmitt, J. Reinigung und Eigenschaften von Acetyl-CoA:D-Aminosäure-α-N-Acetyltransferase aus Hefe. Biochem. Z. 342 (1965) 54–65. [PMID: 5847960]
[EC 2.3.1.36 created 1972]
 
 
EC 2.3.1.37     
Accepted name: 5-aminolevulinate synthase
Reaction: succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2
For diagram of the early stages of porphyrin biosynthesis, click here
Other name(s): ALAS; ALA synthase; α-aminolevulinic acid synthase; δ-aminolevulinate synthase; δ-aminolevulinate synthetase; δ-aminolevulinic acid synthase; δ-aminolevulinic acid synthetase; δ-aminolevulinic synthetase; 5-aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase
Systematic name: succinyl-CoA:glycine C-succinyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-14-3
References:
1.  Bishop, D.F., Henderson, A.S. and Astrin, K.H. Human δ-aminolevulinate synthase - assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X-chromosome. Genomics 7 (1990) 207–214. [PMID: 2347585]
2.  Kikuchi, G., Kumar, A., Talmage, P. and Shemin, D. The enzymatic synthesis of δ-aminolevulinic acid. J. Biol. Chem. 233 (1958) 1214–1219. [PMID: 13598764]
3.  Ramaswamy, N.K. and Nair, P.M. δ-Aminolevulinic acid synthetase from cold-stored potatoes. Biochim. Biophys. Acta 293 (1973) 269–277. [PMID: 4685279]
4.  Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. I. Some properties of the partially purified enzyme. J. Biol. Chem. 247 (1972) 4126–4131. [PMID: 4624703]
5.  Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. II. Studies related to the mechanism of enzyme action and hemin inhibition. J. Biol. Chem. 247 (1972) 4132–4137. [PMID: 5035685]
6.  Tait, G.H. Aminolaevulinate synthetase of Micrococcus denitrificans. Purification and properties of the enzyme, and the effect of growth conditions on the enzyme activity in cells. Biochem. J. 131 (1973) 389–403. [PMID: 4722442]
7.  Warnick, G.R. and Burnham, B.F. Regulation of porphyrin biosynthesis. Purification and characterization of δ-aminolevulinic acid synthase. J. Biol. Chem. 246 (1971) 6880–6885. [PMID: 5315997]
[EC 2.3.1.37 created 1972]
 
 
EC 2.3.1.38     
Accepted name: [acyl-carrier-protein] S-acetyltransferase
Reaction: acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]acetyltransferase; [ACP]acetyltransferase; ACAT; acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase
Systematic name: acetyl-CoA:[acyl-carrier protein] S-acetyltransferase
Comments: This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4]. This is one of the activities associated with β-ketoacyl-ACP synthase III (EC 2.3.1.180) [5].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-16-2
References:
1.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [PMID: 4561013]
2.  Vance, D.E., Mituhashi, O. and Bloch, K. Purification and properties of the fatty acid synthetase from Mycobacterium phlei. J. Biol. Chem. 248 (1973) 2303–2309. [PMID: 4698221]
3.  Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326–2332. [PMID: 5330116]
4.  Lowe, P.N. and Rhodes, S. Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. Biochem. J. 250 (1988) 789–796. [PMID: 3291856]
5.  Tsay, J.T., Oh, W., Larson, T.J., Jackowski, S. and Rock, C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 (1992) 6807–6814. [PMID: 1551888]
6.  Rangan, V.S. and Smith, S. Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J. Biol. Chem. 272 (1997) 11975–11978. [DOI] [PMID: 9115261]
[EC 2.3.1.38 created 1972, modified 2006]
 
 
EC 2.3.1.39     
Accepted name: [acyl-carrier-protein] S-malonyltransferase
Reaction: malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
For diagram of malonate decarboxylase, click here
Other name(s): [acyl carrier protein]malonyltransferase; FabD; malonyl coenzyme A-acyl carrier protein transacylase; malonyl transacylase; malonyl transferase; malonyl-CoA-acyl carrier protein transacylase; malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase; malonyl-CoA:ACP transacylase; malonyl-CoA:ACP-SH transacylase; malonyl-CoA:AcpM transacylase; malonyl-CoA:acyl carrier protein transacylase; malonyl-CoA:acyl-carrier-protein transacylase; malonyl-CoA/dephospho-CoA acyltransferase; MAT; MCAT; MdcH
Systematic name: malonyl-CoA:[acyl-carrier protein] S-malonyltransferase
Comments: This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [7]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [5]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 (biotin-independent malonate decarboxylase) and EC 4.1.1.89 (biotin-dependent malonate decarboxylase). Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [12]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [10] whereas the enzyme from Pseudomonas putida can use both as substrates [11]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4′-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4′-phosphate but in the form of a 2′-(5-triphosphoribosyl)-3′-dephospho-CoA prosthetic group.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37257-17-3
References:
1.  Alberts, A.W., Majerus, P.W. and Vagelos, P.R. Acetyl-CoA acyl carrier protein transacylase. Methods Enzymol. 14 (1969) 50–53.
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [PMID: 4561013]
3.  Williamson, I.P. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases. J. Biol. Chem. 241 (1966) 2326–2332. [PMID: 5330116]
4.  Joshi, V.C. and Wakil, S.J. Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli. Arch. Biochem. Biophys. 143 (1971) 493–505. [DOI] [PMID: 4934182]
5.  Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S. Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J. Biol. Chem. 276 (2001) 27967–27974. [DOI] [PMID: 11373295]
6.  Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure 11 (2003) 147–154. [DOI] [PMID: 12575934]
7.  Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J. Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site. Biochemistry 41 (2002) 1421–1427. [DOI] [PMID: 11814333]
8.  Hoenke, S., Schmid, M. and Dimroth, P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem. 246 (1997) 530–538. [DOI] [PMID: 9208947]
9.  Koo, J.H. and Kim, Y.S. Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem. 266 (1999) 683–690. [DOI] [PMID: 10561613]
10.  Hoenke, S. and Dimroth, P. Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme. Eur. J. Biochem. 259 (1999) 181–187. [PMID: 9914491]
11.  Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. Malonate decarboxylase of Pseudomonas putida is composed of five subunits. FEMS Microbiol. Lett. 169 (1998) 37–43. [DOI] [PMID: 9851033]
12.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 2.3.1.39 created 1972, modified 2006, modified 2008]
 
 


Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald