新型 CMT 酶 TEM-154 的特性分析。
Characterization of the Novel CMT Enzyme TEM-154.
机构信息
Laboratoire de Bactériologie, Faculté de Médecine, 28 Place H. Dunant, 63001 Clermont-Ferrand, France.
出版信息
Antimicrob Agents Chemother. 2011 Mar;55(3):1262-5. doi: 10.1128/AAC.01359-10. Epub 2010 Dec 20.
Abstract
TEM-154, identified in Portugal in 2004, associated the substitutions observed in the extended-spectrum β-lactamase (ESBL) TEM-12 and in the inhibitor-resistant penicillinase (IRT) TEM-33. This enzyme exhibited hydrolytic activity against ceftazidime and a low level of resistance to clavulanic acid. Surprisingly, the substitution Met69Leu enhanced the catalytic efficiency of oxyimino β-lactams conferred by the substitution Arg164Ser. Its discovery confirms the dissemination of the complex mutant group of TEM enzymes in European countries.
摘要
TEM-154 于 2004 年在葡萄牙被鉴定，其结合了在扩展谱β-内酰胺酶（ESBL）TEM-12 和抑制剂抗性青霉素酶（IRT）TEM-33 中观察到的取代。这种酶对头孢他啶具有水解活性，并且对克拉维酸的耐药性较低。令人惊讶的是，取代 Met69Leu 增强了由取代 Arg164Ser 赋予的肟型β-内酰胺的催化效率。它的发现证实了 TEM 酶的复杂突变体群在欧洲国家的传播。
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