4.7 Article

Characterization of the Novel CMT Enzyme TEM-154

Journal

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 55, Issue 3, Pages 1262-1265

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01359-10

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Funding

  1. Ministere de l'Enseignement Superieur et de la Recherche [JE2526]
  2. INRA [USC2018]
  3. Centre Hospitalier Regional Universitaire de Clermont-Ferrand, France
  4. Ministere de la Sante, de la Jeunesse et des Sports

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TEM-154, identified in Portugal in 2004, associated the substitutions observed in the extended-spectrum beta-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 beta-lactams conferred by the substitution Arg164Ser. Its discovery confirms the dissemination of the complex mutant group of TEM enzymes in European countries.

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