TEM-E1: a novel beta-lactamase conferring resistance to ceftazidime

FEMS Microbiol Lett. 1989 May;50(1-2):97-100. doi: 10.1016/0378-1097(89)90466-7.

Abstract

A novel beta-lactamase, conferring resistance to ceftazidime, has been identified to be encoded by a 31 kb plasmid (pUK720) in a clinical E. coli strain isolated in Belgium. The beta-lactamase, new designated TEM-E1, has a pI of approximately 5.4 and lies in between the iso-electric focused bands of the beta-lactamases TEM-1 and TEM-7. The TEM-E1 beta-lactamase has a similar molecular weight of 22,000 to the TEM-1 and it is also inhibited by clavulanic acid. However, the TEM-E1 enzyme differs from TEM-1 by its low rates and efficiency of hydrolysis for ceftazidime and cefotaxime, TEM-E1 has similar efficiency of hydrolysis values for ceftazidime and cefotaxime, but only confers resistance to ceftazidime.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ceftazidime / metabolism
  • Ceftazidime / pharmacology*
  • Conjugation, Genetic
  • Drug Resistance, Microbial
  • Escherichia coli / enzymology
  • Isoelectric Focusing
  • Kinetics
  • Microbial Sensitivity Tests
  • Molecular Weight
  • beta-Lactamases / analysis*

Substances

  • Ceftazidime
  • beta-Lactamases