Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/197/1/85/19110682/197-1-85.pdf
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2. Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor;Concha;Biochemistry,2000
3. The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 à resolution;Ullah;J. Mol. Biol.,1998
4. Role of lysine-67 in the active site of class C β-lactamase from Citrobacter freundii GN346;Tsukamoto;Eur. J. Biochem.,1990
5. Production of single-stranded plasmid DNA;Viera;Methods Enzymol.,1987
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1. Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design;Chemical Reviews;2021-06-15
2. Crystal structures of VIM‐1 complexes explain active site heterogeneity in VIM‐class metallo‐β‐lactamases;The FEBS Journal;2018-11-23
3. Deep Sequencing of Random Mutant Libraries Reveals the Active Site of the Narrow Specificity CphA Metallo-β-Lactamase is Fragile to Mutations;Scientific Reports;2016-09-12
4. Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1;Antimicrobial Agents and Chemotherapy;2016-02
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