(acyl-carrier-protein) S-malonyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a [acyl-carrier-protein] S-malonyltransferase (EC 2.3.1.39) is an enzyme that catalyzes the chemical reaction

malonyl-CoA + [acyl-carrier-protein] $\rightleftharpoons$ CoA + malonyl-[acyl-carrier-protein]

Thus, the two substrates of this enzyme are malonyl-CoA and [[[acyl-carrier-protein]]], whereas its two products are CoA and [[malonyl-[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 malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase. Other names in common use include malonyl coenzyme A-acyl carrier protein transacylase, malonyl transacylase, malonyl transferase, malonyl-CoA-acyl carrier protein transacylase, [acyl carrier protein]malonyltransferase, MAT, FabD, malonyl-CoA:acyl carrier protein transacylase, malonyl-CoA:ACP transacylase, MCAT, and malonyl-CoA:AcpM transacylase. This enzyme participates in fatty acid biosynthesis.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1NM2, 2CUY, 2G1H, 2G2O, 2G2Y, 2G2Z, 2H1Y, 2PFF, 2QC3, and 2QJ3.

[edit] References

IUBMB entry for 2.3.1.39
BRENDA references for 2.3.1.39 (Recommended.)
PubMed references for 2.3.1.39
PubMed Central references for 2.3.1.39
Google Scholar references for 2.3.1.39
Alberts AW, Majerus PW and Vagelos PR (1969). "Acetyl-CoA acyl carrier protein transacylase". Methods Enzymol. 14: 50–53.
Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Adv. Enzymol. Relat. Areas. Mol. Biol. 36: 269–311. PMID 4561013.
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.
Joshi VC, Wakil SJ (1971). "Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli". Arch. Biochem. Biophys. 143: 493–505. doi:10.1016/0003-9861(71)90234-7. PMID 4934182.
Brennan PJ, Minnikin DE, Locht C, Besra GS (2001). "Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II". J. Biol. Chem. 276: 27967–74. doi:10.1074/jbc.M103687200. PMID 11373295.
O'Connell JD 3rd Khosla C, Stroud RM (2003). "Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase". Structure. 11: 147–54. doi:10.1016/S0969-2126(03)00004-2. PMID 12575934.
Szafranska AE, Hitchman TS, Cox RJ, Crosby J, Simpson TJ (2002). "Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site". Biochemistry. 41: 1421–7. doi:10.1021/bi012001p. PMID 11814333.