Citrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties

Biochem J. 1988 Sep 15;254(3):885-90. doi: 10.1042/bj2540885.

Abstract

Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29,000). Their specificity spectrum was rather wide, since they hydrolysed some cephalosporins with kcat: values similar to those observed with the best penicillin substrates. Cloxacillin, methicillin and imipenem were hydrolysed very slowly. Hydrolysis of azthreonam could not be detected.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Cephalosporins / metabolism
  • Chromatography, Affinity
  • Chromosomes, Bacterial / enzymology
  • Citrobacter / enzymology*
  • Electrophoresis, Polyacrylamide Gel
  • Isoelectric Point
  • Isoenzymes / isolation & purification*
  • Kinetics
  • Molecular Weight
  • Penicillins / metabolism
  • Substrate Specificity
  • beta-Lactamases / isolation & purification*

Substances

  • Amino Acids
  • Cephalosporins
  • Isoenzymes
  • Penicillins
  • beta-Lactamases