Related Experiment Video
Updated: Jul 17, 2026

The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018
Biochemical characterisation of the CTX-M-14 beta-lactamase
Yoshikazu Ishii1, Moreno Galleni, Ling Ma
1Centre for Protein Engineering, University of Liège, B6 Institute of Chemistry, Sart Tilman, B4000 Liège, Belgium. yoishii@med.toho-u.ac.jp
Abstract:
Cefotaxime-resistant Escherichia coli TUM1121 was isolated from an abscess of an 83-year-old patient. The CTX-M-14 gene was located on a 70 kb plasmid. The enzyme was purified and its activity was analysed. CTX-M-14 was poorly active against ceftazidime and aztreonam. Aztreonam behaved as a competitive inhibitor. Among the tested suicide substrates for class A beta-lactamases, sulbactam was a rather good substrate. Tazobactam and clavulanic acid behaved as inactivators. The interactions between clavulanic acid and CTX-M-14 were characterised by progressive inactivation of the beta-lactamase. Carbapenems such as imipenem, meropenem or doripenem did not behave as inactivators of CTX-M-14, however very small k(cat) values were observed. This result shows that CTX-M-14 is able to hydrolyse carbapenems.
More Related Videos
07:58Laboratory Techniques Used to Maintain and Differentiate Biotypes of Vibrio cholerae Clinical and Environmental Isolates
Published on: May 30, 2017
09:26Identification of Antibacterial Immunity Proteins in Escherichia coli using MALDI-TOF-TOF-MS/MS and Top-Down Proteomic Analysis
Published on: May 23, 2021
Related Concept Videos
Clinical Significance of Antibiotic Resistance
Mechanism of Antibiotic Resistance in MRSA
Inhibitors of Gram-positive Cell Wall Synthesis