Substitution of aspartic acid-217 of Citrobacter freundii cephalosporinase and properties of the mutant enzymes
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)80250-M/fullpdf
Reference27 articles.
1. A set of bacterial strains for evaluation of .BETA.-lactamase-stability of .BETA.-lactam antibiotics.
2. The structure of β-lactamases
3. Identification of the active site ofCitrobacter freundiiβ-lactamase using dansyl-penicillin
4. Amino Acid Sequence, Active-Site Residue, and Effect of Suicide Inhibitors on Cephalosporinase of Citrobacter freundii GN346
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1. Plasmid-Encoded ACC-4, an Extended-Spectrum Cephalosporinase Variant from Escherichia coli;Antimicrobial Agents and Chemotherapy;2007-10
2. Investigation of the Mechanism of Resistance to Third-Generation Cephalosporins by Class C β-Lactamases by Using Chemical Complementation;ChemBioChem;2005-10-26
3. Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis;Protein Science;2003-08
4. Mutation in Serratia marcescens AmpC β-Lactamase Producing High-Level Resistance to Ceftazidime and Cefpirome;Antimicrobial Agents and Chemotherapy;2001-08
5. Characterization of an Extended-Spectrum Class C β-Lactamase ofCitrobacter freundii;Microbiology and Immunology;2001-04
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