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郭庆丰

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Polyketide synthesis is initiated when acetyl
and malonyl coenzyme A (CoA) are loaded as thioesters on to the 4 ′-phosphopantotheine of
an acyl carrier (ACP) domain by means of the acyltransferase (AT) domain. Condensation then
occurs with another thioester intermediate bound to the ketoacyl CoA synthase (KS) domain,
and decarboxylation of the ACP-bound intermediate occurs. The resulting  β-ketothioester
can then be reduced by the action of the ketoreductase (KR) domain, followed by dehydration
by the dehydratase (DH) domain. If an enoyl reductase (ER) domain is present, an unsaturated
intermediate is formed. Some PKSs contain a methyltransferase (MT) domain that methylates
the  α-carbon of the thioeste
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