Colicin M hydrolyses branched lipids II from Gram-positive bacteria

Biochimie. 2012 Apr;94(4):985-90. doi: 10.1016/j.biochi.2011.12.019. Epub 2011 Dec 26.

Abstract

Lipids II found in some Gram-positive bacteria were prepared in radioactive form from l-lysine-containing UDP-MurNAc-pentapeptide. The specific lateral chains of Enterococcus faecalis, Enterococcus faecium and Staphylococcus aureus (di-L-alanine, D-isoasparagine, and pentaglycine, respectively) were introduced by chemical peptide synthesis using the Fmoc chemistry. The branched nucleotides obtained were converted into the corresponding lipids II by enzymatic synthesis using the MraY and MurG enzymes. All of the lipids were hydrolysed by Escherichia coli colicin M at approximately the same rate as the meso-diaminopimelate-containing lipid II found in Gram-negative bacteria, thereby opening the way to the use of this enzyme as a broad spectrum antibacterial agent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acylation
  • Amino Acids / chemistry
  • Biocatalysis
  • Colicins / chemistry*
  • Esters / chemistry
  • Fluorenes / chemistry
  • Glycolipids / chemical synthesis
  • Glycolipids / chemistry*
  • Glycopeptides / chemical synthesis
  • Glycopeptides / chemistry*
  • Gram-Positive Bacteria*
  • Hydrolysis
  • Substrate Specificity
  • Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives
  • Uridine Diphosphate N-Acetylmuramic Acid / chemistry

Substances

  • Amino Acids
  • Colicins
  • Esters
  • Fluorenes
  • Glycolipids
  • Glycopeptides
  • N(alpha)-fluorenylmethyloxycarbonylamino acids
  • Uridine Diphosphate N-Acetylmuramic Acid
  • peptidoglycolipids
  • UDP-N-acetylmuramic acid pentapeptide