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Information on EC - [acyl-carrier-protein] S-malonyltransferase

for references in articles please use BRENDA:EC2.3.1.39
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IUBMB Comments
This enzyme, along with EC, [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, holo-[acyl-carrier-protein] synthase) is the preferred substrate . This enzyme also forms part of the multienzyme complexes EC, biotin-independent malonate decarboxylase and EC, 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.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
fatty acid synthase, malonyl-coa:acp transacylase, malonyl transferase, mtfabd, hpmcat, fabd2, malonyl-coa:acyl carrier protein transacylase, malonyl coa-acyl carrier protein transacylase, malonyl-coa-acyl carrier protein transacylase, mcamt, more
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
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