Characterization of the Novel CMT Enzyme TEM-154-Reference-Cited by-同舟云学术

Characterization of the Novel CMT Enzyme TEM-154

Published:2011-03 Issue:3 Volume:55 Page:1262-1265
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Robin Frédéric¹²³,Delmas Julien¹²³,Machado Elisabete⁴⁵,Bouchon Bernadette⁶,Peixe Luísa⁴,Bonnet Richard¹²³

Affiliation:

1. CHU Clermont-Ferrand, Centre de Biologie, Laboratoire de bactériologie clinique, Clermont-Ferrand, F-63003 France

2. Clermont, Université, Université d'Auvergne, JE2526 Evolution des bactéries pathogènes et susceptibilité génétique de l'hôte, Clermont-Ferrand, F-63001 France

3. INRA, USC2018, Clermont-Ferrand, France

4. REQUIMTE, Faculdade de Farmácia, Universidade do Porto, Porto, Portugal

5. CEBIMED, Laboratório de Microbiologia, Faculdade de Ciências da Saúde, Universidade Fernando Pessoa, Porto, Portugal

6. Clermont, Université, Université d'Auvergne, INSERM UMR990 Imagerie Moléculaire et Thérapie Vectorisée, Clermont-Ferrand, F-63001 France

Abstract

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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.01359-10

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