(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 | ||||||||
| |||||||||
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] 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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2PFF.
References
[edit]- 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.
