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

J Am Chem Soc. 2011 Aug 31;133(34):13314-6. doi: 10.1021/ja205780g. Epub 2011 Aug 10.


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

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aspergillus nidulans / enzymology*
  • Aspergillus nidulans / genetics*
  • Aspergillus nidulans / metabolism
  • Benzofurans / chemistry
  • Benzofurans / metabolism
  • Biological Products / chemistry
  • Biological Products / metabolism*
  • Polyketide Synthases / genetics*
  • Polyketide Synthases / metabolism
  • Protein Engineering / methods*
  • Protein Structure, Tertiary


  • Benzofurans
  • Biological Products
  • asperfuranone
  • Polyketide Synthases