Biochemical characterization of TEM-92 extended-spectrum beta-lactamase, a protein differing from TEM-52 in the signal peptide.
A bla(TEM-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.
Perilli
Mariagrazia
M
Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, Italy.
Segatore
Bernardetta
B
De Massis
Maria Rosaria
MR
Pagani
Laura
L
Luzzaro
Francesco
F
Rossolini
Gian Maria
GM
Amicosante
Gianfranco
G
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D018550:Cephalosporin Resistance / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D007700:Kinetics; D010403:Penicillin Resistance / Q000235:genetics*; D001618:beta-Lactamases / Q000187:drug effects / Q000235:genetics* / Q000302:isolation & purification; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D047090:beta-Lactams; C445691:TEM-52 beta-lactamase; C434286:beta-lactamase TEM-92; D001618:beta-Lactamases