A natural prodrug activation mechanism in nonribosomal peptide synthesis

Nat Chem Biol. 2011 Sep 18;7(12):888-90. doi: 10.1038/nchembio.688.

Abstract

We have identified a new mechanism for the cleavage and activation of nonribosomally made peptides and peptide-polyketide hybrids that are apparently operational in several different bacteria. This process includes the cleavage of a precursor molecule by a membrane-bound and D-asparagine-specific peptidase, as shown here in the biosynthesis of the antibiotic xenocoumacin from Xenorhabdus nematophila.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / biosynthesis*
  • Anti-Bacterial Agents / chemistry
  • Benzopyrans / chemistry
  • Benzopyrans / metabolism
  • Molecular Conformation
  • Peptide Biosynthesis*
  • Prodrugs / chemistry
  • Prodrugs / metabolism*
  • Stereoisomerism
  • Xenorhabdus / chemistry*

Substances

  • Anti-Bacterial Agents
  • Benzopyrans
  • Prodrugs

Associated data

  • PubChem-Substance/125240901
  • PubChem-Substance/125240902
  • PubChem-Substance/125240903
  • PubChem-Substance/125240904
  • PubChem-Substance/125240905
  • PubChem-Substance/125240906
  • PubChem-Substance/125240907
  • PubChem-Substance/125240908
  • PubChem-Substance/125240909