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.
Perilli, M., Segatore, B., DE MASSIS, M.R., Pagani, L., Luzzaro, F., Rossolini, G.M., et al. (2002). Biochemical characterization of TEM-92 extended-spectrum beta-lactamase: a protein differing from TEM-52 in the signal peptide. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 46(12), 3981-3983 [10.1128/AAC.46.12.3981-3983.2002].
Biochemical characterization of TEM-92 extended-spectrum beta-lactamase: a protein differing from TEM-52 in the signal peptide
ROSSOLINI G. M.;
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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https://hdl.handle.net/11365/8117
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