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Cis-Double bond formation by thioesterase and transfer by ketosynthase in FR901464 biosynthesis.

Authors
  • He, Hai-Yan
  • Tang, Man-Cheng
  • Zhang, Feng
  • Tang, Gong-Li
Type
Published Article
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Publication Date
Mar 26, 2014
Volume
136
Issue
12
Pages
4488–4491
Identifiers
DOI: 10.1021/ja500942y
PMID: 24617828
Source
Medline
License
Unknown

Abstract

Modular polyketide synthases (PKSs) are well known to use ketosynthase (KS)-driven carbon-carbon bond formation, dehydratase-mediated dehydration to form double bonds, and product release by thioesterase (TE), all of which are regarded as the "canonical" roles for most polyketide biosyntheses. FR901464 is biosynthesized by a complex acyltransferase-less PKS system involving a nonterminal TE domain and several mutated KS domains. Here we demonstrate that this TE catalyzes the dehydration of the polyketide intermediate to yield a cis-double bond and a mutated KS transfers the nascent polyketide chain with only a cis-double bond to the downstream acyl carrier protein. These findings not only provide new insights into different enzymatic functions of PKS domains but also suggest an alternative strategy for cis-double bond formation during the polyketide assembly line.

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