Selection and Characterization of Amino Acid Substitutions at Residues 237-240 of TEM-1 β-Lactamase with Altered Substrate Specificity for Aztreonam and Ceftazidime
Open Access
- 1 September 1996
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 271 (37), 22538-22545
- https://doi.org/10.1074/jbc.271.37.22538
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- TEM- and SHV-derived extended-spectrum β-lactamases: relationship between selection, structure and functionJournal of Antimicrobial Chemotherapy, 1995
- TEM β-Lactamase Mutants Hydrolysing Third-generation Cephalosporins: A Kinetic and Molecular Modelling AnalysisJournal of Molecular Biology, 1994
- Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of β‐lactamaseMolecular Microbiology, 1994
- Crystal structure of Escherichia coli TEM1 β‐lactamase at 1.8 Å resolutionProteins-Structure Function and Bioinformatics, 1993
- Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolutionNature, 1992
- Probing β‐lactamase structure and function using random replacement mutagenesisProteins-Structure Function and Bioinformatics, 1992
- Identification of amino acid substitutions that alter the substrate specificity of TEM-1 beta-lactamaseJournal of Bacteriology, 1992
- Extracting information from protein sequences using random replacement mutagenesisMethods, 1991
- Substitution of lysine at position 104 or 240 of TEM-1pTZ18R .beta.-lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonamBiochemistry, 1991
- Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescensInfection, 1983