title: Characterization of the Novel CMT Enzyme TEM-154.
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.
authors.affiliation: Laboratoire de Bactériologie, Faculté de Médecine, 28 Place H. Dunant, 63001 Clermont-Ferrand, France. frobin@chu-clermontferrand.fr
authors.forename: Frédéric
authors.initials: F
authors.lastname: Robin
authors.forename: Julien
authors.initials: J
authors.lastname: Delmas
authors.forename: Elisabete
authors.initials: E
authors.lastname: Machado
authors.forename: Bernadette
authors.initials: B
authors.lastname: Bouchon
authors.forename: Luísa
authors.initials: L
authors.lastname: Peixe
authors.forename: Richard
authors.initials: R
authors.lastname: Bonnet
mesh_terms: D002442:Ceftazidime / Q000378:metabolism; D019818:Clavulanic Acid / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D008969:Molecular Sequence Data; D001618:beta-Lactamases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D004791:Enzyme Inhibitors; D019818:Clavulanic Acid; D002442:Ceftazidime; C088328:beta-lactamase TEM-12; D001618:beta-Lactamases