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.
|Titolo:||Biochemical characterization of TEM-92 extended-spectrum β-lactamase, a protein differing from TEM-52 in the signal peptide|
|Autori interni:||PERILLI, MARIAGRAZIA|
DE MASSIS, MARIA ROSARIA
|Data di pubblicazione:||2002|
|Rivista:||ANTIMICROBIAL AGENTS AND CHEMOTHERAPY|
|Appare nelle tipologie:||1.1 Articolo in rivista|