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Updated: Jun 5, 2026

A Protocol for Functional Assessment of Whole-Protein Saturation Mutagenesis Libraries Utilizing High-Throughput Sequencing
Published on: July 3, 2016
Characterization of the Novel CMT Enzyme TEM-154
Frédéric Robin1, Julien Delmas, Elisabete Machado
1Laboratoire de Bactériologie, Faculté de Médecine, 28 Place H. Dunant, 63001 Clermont-Ferrand, France. frobin@chu-clermontferrand.fr
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.
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