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Engineering of an "unnatural" natural product by swapping polyketide synthase domains in Aspergillus nidulans.

ABSTRACT: An StcA-AfoE hybrid polyketide synthase (PKS), generated by swapping the AfoE (asperfuranone biosynthesis) SAT domain with the StcA (sterigmatocystin biosynthesis) SAT domian, produced a major new metabolite with the same chain length as the native AfoE product. Structure elucidation allowed us to propose a likely pathway, and feeding studies supported the hypothesis that the chain length of PKS metabolites may be under precise control of KS and PT domains.

SUBMITTER: Liu T

PROVIDER: S-EPMC3350771 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Engineering of an "unnatural" natural product by swapping polyketide synthase domains in Aspergillus nidulans.

Liu Ting T Chiang Yi-Ming YM Somoza Amber D AD Oakley Berl R BR Wang Clay C C CC

Journal of the American Chemical Society 20110810 34

An StcA-AfoE hybrid polyketide synthase (PKS), generated by swapping the AfoE (asperfuranone biosynthesis) SAT domain with the StcA (sterigmatocystin biosynthesis) SAT domian, produced a major new metabolite with the same chain length as the native AfoE product. Structure elucidation allowed us to propose a likely pathway, and feeding studies supported the hypothesis that the chain length of PKS metabolites may be under precise control of KS and PT domains. ...[more]

PMID: 21815681

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