Information on EC - 6-deoxyerythronolide-B synthase

for references in articles please use BRENDA:EC2.3.1.94
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IUBMB Comments
The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics. Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3 . The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain . Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP). The KS domain both accepts the growing polyketide chain from the previous module and catalyses the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain. This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms .
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
6-deoxyerythronolide B, 6-deoxyerythronolide B synthase, DEBS, DEBS1, DEBS2, DEBS3, deoxyerythronolide B synthase, deoxyerythronolide B synthase 1, deoxyerythronolide B synthase 2, deoxyerythronolide B synthase 3, more
propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH + 6 H+ = 6-deoxyerythronolide B + 7 CoA + 6 CO2 + H2O + 6 NADP+
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