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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Aspergillus nidulans / enzymology*
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Aspergillus nidulans / genetics*
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Aspergillus nidulans / metabolism
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Benzofurans / chemistry
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Benzofurans / metabolism
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Biological Products / chemistry
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Biological Products / metabolism*
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Polyketide Synthases / genetics*
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Polyketide Synthases / metabolism
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Protein Engineering / methods*
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Protein Structure, Tertiary
Substances
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Benzofurans
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Biological Products
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asperfuranone
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Polyketide Synthases