Abstract
Lysobacter are ubiquitous in the environment but remain largely underexplored, although the bacteria are considered "peptide specialists". Here, we identified a new cyclic lipodepsipeptide, WBP-29479A1 (1), through genome mining of L. antibioticus ATCC 29479. 1 is biosynthesized by a large NRPS gene cluster, and its structure, including the six nonproteinogenic residues and 3-hydroxy fatty acid, was determined by extensive spectroscopic analyses and chemical derivatization. 1 exhibits potent anti-MRSA activity in a menaquinone-dependent manner.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / metabolism
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Anti-Bacterial Agents / pharmacology*
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Depsipeptides / chemistry
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Depsipeptides / pharmacology
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Genome, Bacterial
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Hemolytic Agents / chemistry
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Hemolytic Agents / pharmacology
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Humans
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Lysobacter / genetics*
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Lysobacter / metabolism
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Methicillin-Resistant Staphylococcus aureus / drug effects
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Microbial Sensitivity Tests
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Molecular Structure
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Multigene Family
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Mutation
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Peptide Synthases / genetics
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Peptide Synthases / metabolism
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Valine
Substances
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Anti-Bacterial Agents
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Depsipeptides
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Hemolytic Agents
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Peptide Synthases
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non-ribosomal peptide synthase
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Valine