A blaTEM-92 gene was cloned from a Proteus mirabilis isolate and expressed in Escherichia coli. Production of the enzyme caused reduction of susceptibility to penicillins and narrow- to expanded-spectrum cephalosporins but not to moxalactam and cephamycins. Determination of kinetic parameters with the purified enzyme revealed hydrolysis of expanded-spectrum cephalosporins, while cephamycins, moxalactam, and aztreonam were very poorly or not hydrolyzed. Clavulanate and penicillanic acid sulfones acylated TEM-92 slowly, and deacylation occurred at measurable rates.

Biochemical characterization of TEM-92 extended-spectrum β-lactamase, a protein differing from TEM-52 in the signal peptide

PERILLI, MARIAGRAZIA;SEGATORE, Bernardetta;DE MASSIS, MARIA ROSARIA;AMICOSANTE, Gianfranco
2002-01-01

Abstract

A blaTEM-92 gene was cloned from a Proteus mirabilis isolate and expressed in Escherichia coli. Production of the enzyme caused reduction of susceptibility to penicillins and narrow- to expanded-spectrum cephalosporins but not to moxalactam and cephamycins. Determination of kinetic parameters with the purified enzyme revealed hydrolysis of expanded-spectrum cephalosporins, while cephamycins, moxalactam, and aztreonam were very poorly or not hydrolyzed. Clavulanate and penicillanic acid sulfones acylated TEM-92 slowly, and deacylation occurred at measurable rates.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/7185
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