EC 18.104.22.168 - [acyl-carrier-protein] S-malonyltransferase
IntEnz Enzyme Nomenclature
malonyl coenzyme A-acyl carrier protein transacylase
malonyl-CoA-acyl carrier protein transacylase
malonyl-CoA:acyl carrier protein transacylase
acyl carrier protein malonyltransferase
- malonyl-CoA + an acyl-carrier-protein = CoA + a malonyl-acyl-carrier-protein
This enzyme, along with EC 22.214.171.124, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis . The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 126.96.36.199, holo-[acyl-carrier-protein] synthase) is the preferred substrate . This enzyme also forms part of the multienzyme complexes EC 188.8.131.52 (biotin-independent malonate decarboxylase) and EC 184.108.40.206 (biotin-dependent malonate decarboxylase). Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase . In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot  whereas the enzyme from Pseudomonas putida can use both as substrates . The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
Links to other databases
Acetyl-CoA acyl carrier protein transacylase.Methods Enzymol. 14 : 50-53 (1969).
Acyl carrier protein.Adv. Enzymol. Relat. Areas Mol. Biol. 36 : 269-311 (1972). [PMID: 4561013]
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 : 2326-2332 (1966). [PMID: 5330116]
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 (1971). [PMID: 4934182]
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 : 27967-27974 (2001). [PMID: 11373295]
Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase.Structure 11 : 147-154 (2003). [PMID: 12575934]
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 : 1421-1427 (2002). [PMID: 11814333]
Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli.Eur. J. Biochem. 246 : 530-538 (1997). [PMID: 9208947]
Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus.Eur. J. Biochem. 266 : 683-690 (1999). [PMID: 10561613]
Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzymeEur. J. Biochem. 259 : 181-187 (1999). [PMID: 9914491]
Erratum report: Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzymeEur. J. Biochem. 259 : 259 (1999).
Malonate decarboxylase of Pseudomonas putida is composed of five subunits.FEMS Microbiol. Lett. 169 : 37-43 (1998). [PMID: 9851033]
Enzymic and genetic basis for bacterial growth on malonate.Mol. Microbiol. 25 : 3-10 (1997). [PMID: 11902724]
[EC 220.127.116.11 created 1972, modified 2006, modified 2008]