EC 2.3.1.38 - [acyl-carrier-protein] S-acetyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.38

Names

Accepted name:
[acyl-carrier-protein] S-acetyltransferase
Other names:
[ACP]acetyltransferase
[acyl-carrier-protein]acetyltransferase
acetyl coenzyme A-acyl-carrier-protein transacylase
ACAT
ACP acetyltransferase
acyl-carrier-protein acetyltransferase
Systematic name:
acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004313
CAS Registry Number: 37257-16-2
UniProtKB/Swiss-Prot: (11) [show] [UniProt]

References

  1. Prescott, D.J. and Vagelos, P.R.
    Acyl carrier protein.
    Adv. Enzymol. Relat. Areas Mol. Biol. 36: 269-311 (1972). [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: 2303-2309 (1973). [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: 2326-2332 (1966). [PMID: 5330116]
  4. Lowe, P.N. and Rhodes, S.
    Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli.
    Biochem. J. 250: 789-796 (1988). [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: 6807-6814 (1992). [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: 11975-11978 (1997). [PMID: 9115261]

[EC 2.3.1.38 created 1972, modified 2006]