TEM-92超广谱β-内酰胺酶的生化特性，一种信号肽不同于TEM-52的蛋白质。
Biochemical characterization of TEM-92 extended-spectrum beta-lactamase, a protein differing from TEM-52 in the signal peptide.
作者信息
Perilli Mariagrazia, Segatore Bernardetta, De Massis Maria Rosaria, Pagani Laura, Luzzaro Francesco, Rossolini Gian Maria, Amicosante Gianfranco
机构信息
Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, Italy.
出版信息
Antimicrob Agents Chemother. 2002 Dec;46(12):3981-3. doi: 10.1128/AAC.46.12.3981-3983.2002.
Abstract
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.
摘要
从一株奇异变形杆菌分离株中克隆出bla(TEM-92)基因，并在大肠杆菌中表达。该酶的产生导致对青霉素和窄谱至广谱头孢菌素的敏感性降低，但对莫西沙星和头霉素不敏感。用纯化的酶测定动力学参数表明，广谱头孢菌素可被水解，而头霉素、莫西沙星和氨曲南很少被水解或不被水解。克拉维酸和青霉素烷砜对TEM-92的酰化作用缓慢，且脱酰化以可测量的速率发生。
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