InterPro domain: IPR014030

Beta-ketoacyl-ACP synthase 2.3.1.41 (KAS) [ 1 ] is the enzyme that catalyzesthe condensation of malonyl-ACP with the growing fatty acid chain. It is found as a componentof a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyzes theformation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from Penicillium patulum [ 2 ], which isinvolved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzymesystems; Emericella nidulans multifunctional protein Wa, which is involved in the biosynthesisof conidial green pigment; Rhizobium nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeastmitochondrial protein CEM1. The condensation reaction is a two step process, first the acylcomponent of an activated acyl primer is transferred to a cysteine residue of the enzyme andis then condensed with an activated malonyl donor with the concomitant release of carbondioxide.

This entry represents the N-terminal domain of beta-ketoacyl-ACP synthases.

1. beta-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Carlsberg Res. Commun. 53, 357-70
2. The multifunctional 6-methylsalicylic acid synthase gene of Penicillium patulum. Its gene structure relative to that of other polyketide synthases. Eur. J. Biochem. 192, 487-98