Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci

FEMS Microbiol Lett. 1992 Jul 1;73(1-2):195-200. doi: 10.1016/0378-1097(92)90608-q.


Cytoplasmic precursors of the peptidoglycan biosynthetic pathway were purified from vancomycin-treated, glycopeptide-sensitive and -resistant strains of Enterococcus faecium. Resistance was due to production of a modified precursor, UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-lactate, where lactate was identified on the basis of mass of the precursor and on its ability to act as a substrate for D-lactate dehydrogenase after release from the precursor. The presence of the D-lactate residue instead of D-alanine in the terminal position would hinder formation of a vancomycin-precursor complex, without preventing incorporation of the precursor into mature peptidoglycan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Wall / chemistry
  • Cytoplasm / chemistry
  • Drug Resistance, Microbial
  • Enterococcus faecium / drug effects
  • Enterococcus faecium / metabolism*
  • Glycopeptides / pharmacology*
  • Hexosamines / analysis
  • Mass Spectrometry
  • Molecular Sequence Data
  • Peptidoglycan / biosynthesis*
  • Protein Precursors / biosynthesis*
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives
  • Uridine Diphosphate N-Acetylmuramic Acid / analysis
  • Vancomycin / pharmacology


  • Glycopeptides
  • Hexosamines
  • Peptidoglycan
  • Protein Precursors
  • Uridine Diphosphate N-Acetylmuramic Acid
  • UDP-N-acetylmuramyl-Ala-Glu-Lys-Ala-lactate
  • Vancomycin