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Characterization of the Novel CMT Enzyme TEM-154.

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

SUBMITTER: Robin F

PROVIDER: S-EPMC3067075 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Characterization of the Novel CMT Enzyme TEM-154.

Robin Frédéric F Delmas Julien J Machado Elisabete E Bouchon Bernadette B Peixe Luísa L Bonnet Richard R

Antimicrobial agents and chemotherapy 20101220 3

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 ...[more]

PMID: 21173189

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