Substrate recognition and channeling of monomodules from the pikromycin polyketide synthase

Brian J. Beck, Courtney C. Aldrich, Robert A. Fecik, Kevin A. Reynolds, David H. Sherman

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

The unique ability of the pikromycin (Pik) polyketide synthase to generate 12- and 14-membered ring macrolactones presents an opportunity to explore the fundamental processes underlying polyketide synthesis, specifically the mechanistic details of the chain extension process. We have overexpressed and purified PikAIII (module 5) and PikAIV (module 6) and assessed the ability of these proteins to generate tri- and tetraketide lactone products using N-acetylcysteamine-activated diketides and 14C-methylmalonyl-CoA as substrates. Comparison of the stereochemical specificities for PikAIII and PikAIV and the reported values for the DEBS modules reveals significant differences between these systems.

Original languageEnglish (US)
Pages (from-to)12551-12557
Number of pages7
JournalJournal of the American Chemical Society
Volume125
Issue number41
DOIs
StatePublished - Oct 15 2003

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