| Type: | Domain | Name: | Polyketide synthase, beta-ketoacyl synthase domain |
| Description: | Beta-ketoacyl-ACP synthase (KAS) [] is the enzyme that catalyzesthe condensation of malonyl-ACP with the growing fatty acid chain. It is found as a component of 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[], which isinvolved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; Emericella nidulansmultifunctional protein Wa, which is involved in the biosynthesis of 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 yeast mitochondrial 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 and is then condensed with an activated malonyl donor with the concomitant release of carbondioxide.This entry represents the the beta-ketoacyl synthase region from a number of polyketide synthases including erythronolide synthase and the lovastatin nonaketide chain synthase. | Short Name: | PKS_Beta-ketoAc_synthase_dom |
