Kinetic Properties and Metal Content of the Metallo-β-lactamase CcrA Harboring Selective Amino Acid Substitutions
Open Access
- 1 May 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (22) , 15706-15711
- https://doi.org/10.1074/jbc.274.22.15706
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Dsb-insensitive expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrAJournal of Bacteriology, 1996
- Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilisStructure, 1996
- Characterization of the Metal-Binding Sites of the β-Lactamase from Bacteroides fragilisBiochemistry, 1996
- Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of beta-lactams in three Bacteroides fragilis isolates that harbor a metallo-beta-lactamase geneAntimicrobial Agents and Chemotherapy, 1994
- An overview of the kinetic parameters of class B β-lactamasesBiochemical Journal, 1993
- Kinetic interactions of tazobactam with beta-lactamases from all major structural classesAntimicrobial Agents and Chemotherapy, 1993
- Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636Antimicrobial Agents and Chemotherapy, 1992
- Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragiiis metallo‐β‐lactamase gene, ccrAMolecular Microbiology, 1991
- Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilisAntimicrobial Agents and Chemotherapy, 1991
- Metal cofactor requirement of β-lactamase IIBiochemical Journal, 1974