The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes

FEBS Lett. 1996 Aug 26;392(2):184-8. doi: 10.1016/0014-5793(96)00809-5.


Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species. Here we report the cloning of the homologous Escherichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • DNA Primers
  • Escherichia coli / enzymology*
  • Glycosyltransferases / chemistry
  • Glycosyltransferases / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Peptidoglycan / biosynthesis*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Species Specificity


  • DNA Primers
  • Membrane Proteins
  • Peptidoglycan
  • Recombinant Proteins
  • Glycosyltransferases

Associated data

  • GENBANK/L19300
  • GENBANK/L42023
  • GENBANK/U18997
  • GENBANK/Z22737