TEM-158 (CMT-9), a new member of the CMT-type extended-spectrum beta-lactamases.
TEM-158 was found to include the substitutions previously observed for TEM-12 and TEM-35. This enzyme presented hydrolytic activity against ceftazidime and a high level of resistance against clavulanate, which can alter its detection. Its discovery highlights the need for accurate detection methods.
Robin
Frédéric
F
CHU Clermont-Ferrand, Centre de Biologie, Laboratoire de bactériologiecinique, Faculté de Médecine, 28 place H. Dunant, 63001 Clermont-Ferrand, France. frobin@chu-clermontferrand.fr
Delmas
Julien
J
Brebion
Amélie
A
Dubois
Damien
D
Constantin
Jean-Michel
JM
Bonnet
Richard
R
D002384:Catalysis; D002442:Ceftazidime / Q000494:pharmacology; D019818:Clavulanic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D018440:beta-Lactam Resistance / Q000235:genetics; D001618:beta-Lactamases / Q000235:genetics / Q000378:metabolism*; D047090:beta-Lactams / Q000378:metabolism / Q000494:pharmacology
D029968:Escherichia coli Proteins; D007527:Isoenzymes; D047090:beta-Lactams; D019818:Clavulanic Acid; D002442:Ceftazidime; D001618:beta-Lactamases; C525735:beta-lactamase TEM-158, E coli
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