(acyl-carrier-protein) S-acetyltransferase

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In enzymology, a [acyl-carrier-protein] S-acetyltransferase (EC 2.3.1.38) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + [acyl-carrier-protein] CoA + acetyl-[acyl-carrier-protein]

Thus, the two substrates of this enzyme are acetyl-CoA and acyl-carrier-protein, whereas its two products are CoA and acetyl-acyl-carrier-protein.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, [acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PFF.

References

  • IUBMB entry for 2.3.1.38
  • BRENDA references for 2.3.1.38 (Recommended.)
  • PubMed references for 2.3.1.38
  • PubMed Central references for 2.3.1.38
  • Google Scholar references for 2.3.1.38
  • Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Adv. Enzymol. Relat. Areas. Mol. Biol. 36: 269–311. PMID 4561013. 
  • Vance DE, Mitsuhashi O, Bloch K (1973). "Purification and properties of the fatty acid synthetase from Mycobacterium phlei". J. Biol. Chem. 248: 2303–9. PMID 4698221. 
  • Williamson IP, Wakil SJ (1966). "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: 2326–32. PMID 5330116. 
  • Lowe PN, Rhodes S (1988). "Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli". Biochem. J. 250: 789–96. PMID 3291856. 
  • Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO (1992). "Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12". J. Biol. Chem. 267: 6807–14. PMID 1551888. 
  • Rangan VS, Smith S (1997). "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: 11975–8. PMID 9115261. 

External links

The CAS registry number for this enzyme class is 37257-16-2.

Gene Ontology (GO) codes



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