NMC-Aβ-内酰胺酶的动力学研究，一种也能水解头孢霉素的安布勒A类碳青霉烯酶。
A kinetic study of NMC-A beta-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins.
作者信息
Mariotte-Boyer S, Nicolas-Chanoine M H, Labia R
机构信息
Service de Bactériologie-Virologie, Hôpital Lariboisière, Paris, France.
出版信息
FEMS Microbiol Lett. 1996 Sep 15;143(1):29-33. doi: 10.1111/j.1574-6968.1996.tb08457.x.
In order to analyze its kinetic parameters, an Ambler class A carbapenemase NMC-A was purified. NMC-A demonstrated unusually strong hydrolytic activity towards imipenem and meropenem. Moreover, it hydrolyzed cephamycins with kcat values uncommonly high for this class of beta-lactamases. Clavulanic acid and tazobactam had comparable inhibitory activity against NMC-A, whereas sulbactam was the least active inhibitor. Noticeably, NMC-A was more readily inhibited by brobactam. All these catalytic properties suggest that NMC-A possesses an original structure of its active site allowing hydrolysis of beta-lactams usually stable to the hydrolytic activity of class A beta-lactamases.
为了分析其动力学参数，纯化了一种安布勒A类碳青霉烯酶NMC-A。NMC-A对亚胺培南和美罗培南表现出异常强的水解活性。此外，它能水解头孢霉素，其催化常数（kcat）值对于这类β-内酰胺酶来说异常高。克拉维酸和他唑巴坦对NMC-A具有相当的抑制活性，而舒巴坦是活性最低的抑制剂。值得注意的是，NMC-A更容易被溴巴坦抑制。所有这些催化特性表明，NMC-A的活性位点具有独特结构，使其能够水解通常对A类β-内酰胺酶水解活性稳定的β-内酰胺类药物。
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