The ponA gene of Enterococcus faecalis JH2-2 codes for a low-affinity class A penicillin-binding protein

J Bacteriol. 2004 Jul;186(13):4412-6. doi: 10.1128/JB.186.13.4412-4416.2004.

Abstract

A soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 (*PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli 14C-labeled lipid II precursor. As a DD- peptidase, it could hydrolyze thiolester substrates with efficiencies similar to those of other class A penicillin-binding proteins (PBPs) and bind beta-lactams, but with k2/K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Bacterial Proteins*
  • Base Sequence
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Enterococcus faecalis / genetics*
  • Genes, Bacterial*
  • Glycosyltransferases / metabolism
  • Kinetics
  • Molecular Sequence Data
  • Penicillin-Binding Proteins*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Carrier Proteins
  • Penicillin-Binding Proteins
  • Glycosyltransferases

Associated data

  • GENBANK/AJ302065