NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
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Title
NDM-1, the ultimate promiscuous enzyme: substrate recognition and catalytic mechanism
Authors
Keywords
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Journal
FASEB JOURNAL
Volume 27, Issue 5, Pages 1917-1927
Publisher
FASEB
Online
2013-01-31
DOI
10.1096/fj.12-224014
References
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Related references
Note: Only part of the references are listed.- Mechanistic and Spectroscopic Studies of Metallo-β-lactamase NDM-1
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- (2010) Olga Khersonsky and Dan S. Tawfik Annual Review of Biochemistry
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- NDM-1 — A Cause for Worldwide Concern
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- (2009) K. Bush et al. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
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- Common Mechanistic Features among Metallo-β-lactamases
- (2009) Fabio Simona et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mutational analysis of the zinc- and substrate-binding sites in the CphA metallo-β-lactamase fromAeromonas hydrophila
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- Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase
- (2008) M. P. Blakeley et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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