NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli
NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli
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DOI：
10.1128/aac.05961-11
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发表时间：
2012-04-01
影响因子：
4.9
通讯作者：
Poirel, Laurent
中科院分区：
文献类型：
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作者：
Nordmann, Patrice;Boulanger, Anne E.;Poirel, Laurent
对所有 β-内酰胺（包括碳青霉烯类）耐药的临床大肠杆菌分离株表达一种新型金属-β-内酰胺酶 (MBL) NDM-4，与 NDM-1 的区别在于单个氨基酸取代 (Met154Leu)。与 NDM-1 相比，NDM-4 对碳青霉烯类和几种头孢菌素具有增强的水解活性。该氨基酸取代并不位于 NDM-1 的已知活性位点，表明远程氨基酸取代也可能在该 MBL 的延长活性中发挥作用。
A clinical Escherichia coli isolate resistant to all beta-lactams, including carbapenems, expressed a novel metallo-beta-lactamase (MBL), NDM-4, differing from NDM-1 by a single amino acid substitution (Met154Leu). NDM-4 possessed increased hydrolytic activity toward carbapenems and several cephalosporins compared to that of NDM-1. This amino acid substitution was not located in the known active sites of NDM-1, indicating that remote amino acid substitutions might also play a role in the extended activity of this MBL.