FIGURE 2 | Fungal polyketide synthase (PKS) domain structure.

From the following article:

Fungal secondary metabolism — from biochemistry to genomics

Nancy P. Keller, Geoffrey Turner & Joan W. Bennett

Nature Reviews Microbiology 3, 937-947 (December 2005)

doi:10.1038/nrmicro1286

Fungal secondary metabolism |[mdash]| from biochemistry to genomics

The minimal structure is KS–AT–ACP. Optional domains are in brackets. 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 beta-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 alpha-carbon of the thioester. CYC, cyclase; TE, thioesterase.

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