Characterization of the Novel CMT Enzyme TEM-154

Antimicrob Agents Chemother. 2011 Mar;55(3):1262-5. doi: 10.1128/AAC.01359-10. Epub 2010 Dec 20.

Abstract

TEM-154, identified in Portugal in 2004, associated the substitutions observed in the extended-spectrum β-lactamase (ESBL) TEM-12 and in the inhibitor-resistant penicillinase (IRT) TEM-33. This enzyme exhibited hydrolytic activity against ceftazidime and a low level of resistance to clavulanic acid. Surprisingly, the substitution Met69Leu enhanced the catalytic efficiency of oxyimino β-lactams conferred by the substitution Arg164Ser. Its discovery confirms the dissemination of the complex mutant group of TEM enzymes in European countries.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ceftazidime / metabolism
  • Clavulanic Acid / pharmacology
  • Enzyme Inhibitors / pharmacology
  • Molecular Sequence Data
  • beta-Lactamases / chemistry*
  • beta-Lactamases / genetics
  • beta-Lactamases / metabolism*

Substances

  • Enzyme Inhibitors
  • Clavulanic Acid
  • Ceftazidime
  • beta-lactamase TEM-12
  • beta-Lactamases

Associated data

  • GENBANK/FJ807656