Biology:(acyl-carrier-protein) S-acetyltransferase
| [acyl-carrier-protein] S-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.3.1.38 | ||||||||
| CAS number | 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 | ||||||||
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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] [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "Acyl carrier protein". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. 36. 1972. pp. 269–311. doi:10.1002/9780470122815.ch8. ISBN 9780470122815.
- "Purification and properties of the fatty acid synthetase from Mycobacterium phlei". J. Biol. Chem. 248 (7): 2303–9. 1973. PMID 4698221.
- "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. 1966. PMID 5330116.
- "Purification and characterization of acyl-carrier-protein acetyltransferase from Escherichia coli". Biochem. J. 250 (3): 789–96. 1988. doi:10.1042/bj2500789. PMID 3291856.
- "Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12". J. Biol. Chem. 267 (10): 6807–14. 1992. PMID 1551888.
- "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. 1997. doi:10.1074/jbc.272.18.11975. PMID 9115261.
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