A new type of tripropeptin with anteiso-branched chain fatty acid from Lysobacter sp. BMK333-48F3

J Antibiot (Tokyo). 2008 Sep;61(9):577-82. doi: 10.1038/ja.2008.78.

Abstract

Branched chain amino acids are often utilized as the precursors of many lipid-containing bacterial secondary metabolites. The effect of isoleucine on the composition of the mixture of cyclic lipopeptide antibiotics, tripropeptins from Lysobacter sp. BMK333-48F3 was evaluated. As expected, a novel tripropeptin analog with an anteiso-branched fatty acid was produced. The new compound, TPPaiC shows potent antibacterial activity against Gram-positive bacteria including MRSA and VRE. On the other hand, no increase was observed in the production of other tripropeptins by the addition of isoleucine.

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / isolation & purification*
  • Anti-Bacterial Agents / pharmacology
  • Depsipeptides / chemistry
  • Depsipeptides / isolation & purification*
  • Depsipeptides / pharmacology
  • Fatty Acids / chemistry
  • Fatty Acids / isolation & purification*
  • Fatty Acids / pharmacology
  • Fermentation
  • Lysobacter / metabolism*
  • Magnetic Resonance Spectroscopy

Substances

  • Anti-Bacterial Agents
  • Depsipeptides
  • Fatty Acids
  • tripropeptin aiC