(acyl-carrier-protein) S-acetyltransferase

[acyl-carrier-protein] S-acetyltransferase
Identifiers
EC no.	2.3.1.38
CAS no.	37257-16-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

acetyl-CoA + [acyl-carrier-protein] ${\displaystyle \rightleftharpoons }$ 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, acetyl-CoA:ACP 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

• Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 36. pp. 269–311. doi:10.1002/9780470122815.ch8. ISBN 9780470122815. PMID 4561013.
• Vance DE, Mitsuhashi O, Bloch K (1973). "Purification and properties of the fatty acid synthetase from Mycobacterium phlei". J. Biol. Chem. 248 (7): 2303–9. doi:10.1016/S0021-9258(19)44110-0. 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 (10): 2326–32. doi:10.1016/S0021-9258(18)96625-1. PMID 5330116.
• Lowe PN, Rhodes S (1988). "Purification and characterization of acyl-carrier-protein acetyltransferase from Escherichia coli". Biochem. J. 250 (3): 789–96. doi:10.1042/bj2500789. PMC 1148925. PMID 3291856.
• Tsay JT, Oh W, Larson TJ, Jackowski S, Rock CO (1992). "Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12". J. Biol. Chem. 267 (10): 6807–14. doi:10.1016/S0021-9258(19)50498-7. 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 (18): 11975–8. doi:10.1074/jbc.272.18.11975. PMID 9115261.