NDM-4 Metallo-β-Lactamase with Increased Carbapenemase Activity from Escherichia coli
2012 ◽
Vol 56
(4)
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pp. 2184-2186
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Keyword(s):
ABSTRACTA clinicalEscherichia coliisolate resistant to all β-lactams, including carbapenems, expressed a novel metallo-β-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.
2014 ◽
Vol 59
(1)
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pp. 450-460
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1990 ◽
Vol 265
(36)
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pp. 22520-22525
Keyword(s):
2001 ◽
Vol 45
(12)
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pp. 3591-3594
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2005 ◽
Vol 349
(2)
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pp. 413-423
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2006 ◽
Vol 60
(4)
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pp. 939-950
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2000 ◽
Vol 182
(9)
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pp. 2567-2573
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1996 ◽
Vol 178
(15)
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pp. 4731-4733
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1994 ◽
Vol 7
(12)
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pp. 1495-1500
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Keyword(s):
1986 ◽
Vol 189
(1)
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pp. 227-238
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