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. Copyright © 2011, American Society for Microbiology. All Rights Reserved.
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CITATION STYLE
Robin, F., Delmas, J., Machado, E., Bouchon, B., Peixe, L., & Bonnet, R. (2011). Characterization of the novel CMT enzyme TEM-154. Antimicrobial Agents and Chemotherapy, 55(3), 1262–1265. https://doi.org/10.1128/AAC.01359-10
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