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
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / biosynthesis*
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Anti-Bacterial Agents / chemistry
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Benzopyrans / chemistry
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Benzopyrans / metabolism
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Molecular Conformation
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Peptide Biosynthesis*
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Prodrugs / chemistry
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Prodrugs / metabolism*
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Stereoisomerism
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Xenorhabdus / chemistry*
Substances
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Anti-Bacterial Agents
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Benzopyrans
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Prodrugs
Associated data
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PubChem-Substance/125240901
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PubChem-Substance/125240902
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PubChem-Substance/125240903
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PubChem-Substance/125240904
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PubChem-Substance/125240905
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PubChem-Substance/125240906
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PubChem-Substance/125240907
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PubChem-Substance/125240908
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PubChem-Substance/125240909