Mutasynthesis of enterocin and wailupemycin analogues

John A. Kalaitzis, Miho Izumikawa, Longkuan Xiang, Christian Hertweck, Bradley S. Moore*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)

Abstract

Inactivation of the novel phenylalanine ammonia lyase gene encP, whose product is a key component in the biosynthetic pathway to benzoyl-coenzyme A (CoA) in the bacterium Streptomyces maritimus, resulted in the loss of production of the benzoate-primed polyketides enterocin and wailupemycin G. A series of cinnamate and benzoate derivatives were administered to the ΔencP mutant, resulting in the formation of novel analogues bearing p-fluorobenzoate, 2- and 3-thiophenecarboxylate, and cyclohex-1-enecarboxylate residues. Given that the benzoate:CoA ligase EncN was evaluated to have broad in vitro substrate specificity towards aryl acids, the strict starter unit specificity observed in vivo indicates that the enterocin type II polyketide synthase (PKS) exerts selective control over the choice of starter units. This study represents the first mutasynthesis experiments with iterative type II PKSs.

Original languageEnglish
Pages (from-to)9290-9291
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number31
DOIs
Publication statusPublished - 2003
Externally publishedYes

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