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Characterization of the ketosynthase and acyl carrier protein domains at the Lnml nonribosomal peptide synthetase-polyketide synthase interface for leinamycin biosynthesis

Academic Article
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Overview

authors

  • Huang, Y.
  • Tang, G. L.
  • Pan, G.
  • Chang, C. Y.
  • Shen, Ben

publication date

  • 2016

journal

  • Organic Letters  Journal

abstract

  • Leinamycin (LNM) is biosynthesized by a hybrid nonribosomal peptide synthetase (NRPS)-acyltransferase (AT)-less type I polyketide synthase (PKS). Characterization of LnmI revealed ketosynthase (KS)-acyl carrier protein (ACP)-KS domains at the NRPS-PKS interface. Inactivation of the KS domain or ACP domain in vivo abolished LNM production, and the ACP domain can be phosphopantetheinylated in vitro. The LnmI KS-ACP-KS architecture represents a new mechanism for functional crosstalk between NRPS and AT-less type I PKS in the biosynthesis of hybrid peptide-polyketide natural products.
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Identity

PubMed Central ID

  • PMC5013926

International Standard Serial Number (ISSN)

  • 1523-7060

Digital Object Identifier (DOI)

  • 10.1021/acs.orglett.6b02033

PubMed ID

  • 27541042
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Additional Document Info

start page

  • 4288

end page

  • 4291

volume

  • 18

issue

  • 17

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