Polyunsaturated fatty-acid-like trans-enoyl reductases utilized in polyketide biosynthesis

Stefanie B. Bumpus, Nathan A. Magarvey, Neil L. Kelleher, Christopher T. Walsh, Christopher T. Calderone

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


Polyketide biosynthesis is typically directed by cis-acting catalytic domains. In the case of the Bacillus subtilis secondary metabolite dihydrobacillaene, the cis-acting domains are not sufficient to generate the saturated C14′-C15′ bond. In this communication, we identify PksE as a trans-acting enoyl reductase utilized in the biosynthesis of this portion of dihydrobacillaene. PksE is homologous to the enzymes predicted to serve as enoyl reductases in polyunsaturated fatty acid (PUFA) biosynthesis, and we confirmed this functional assignment in vitro. These results suggest a general enoyl reduction pathway in polyketide biosynthesis and a means by which PUFA-like biosynthetic machinery can modulate small-molecule function.

Original languageEnglish (US)
Pages (from-to)11614-11616
Number of pages3
JournalJournal of the American Chemical Society
Issue number35
StatePublished - Sep 3 2008

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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