Characterization of three different lytic transglycosylases in Escherichia coli

FEMS Microbiol Lett. 1993 Aug 1;111(2-3):141-6. doi: 10.1111/j.1574-6968.1993.tb06376.x.

Abstract

Two lytic transglycosylases, releasing 1,6-anhydromuropeptides from murein sacculi are present in a mutant deleted for the soluble lytic transglycosylase 70 (Slt70). Thus, there are three different lytic transglycosylases in Escherichia coli. One of the remaining enzymes is soluble and one is a membrane protein that can be solubilized by 2% Triton X-100 in 0.5 M NaCl. Both enzymes are exo-muramidases. Only the membrane enzyme, but not the soluble ones, hydrolyses isolated murein glycan strands (poly-GlcNAc-MurNAc). While the soluble enzymes are inhibited by the muropeptide TetraTriLysArg(dianhydro), the membrane enzyme is not. The antibiotic bulgecin that inhibits Slt70 does not inhibit the lytic transglycosylases present in the slt70 deletion mutant.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Glycopeptides / pharmacology
  • Glycosyltransferases*
  • Kinetics
  • Membranes / enzymology
  • Molecular Sequence Data
  • Peptidoglycan / chemistry
  • Solubility
  • Substrate Specificity
  • Transferases / antagonists & inhibitors
  • Transferases / genetics
  • Transferases / metabolism*

Substances

  • Glycopeptides
  • Peptidoglycan
  • bulgecin
  • Transferases
  • Glycosyltransferases
  • murein transglycosylase