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] |
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For diagram of malonate decarboxylase, click here |
Other name(s): |
acetyl coenzyme A-acyl-carrier-protein transacylase; [acyl-carrier-protein]-acetyltransferase; [ACP]-acetyltransferase; 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-[acyl-carrier-protein] 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] |
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[EC 2.3.1.38 created 1972, modified 2006] |
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