β-Lactamases are the main cause of bacterial resistance to penicillins, cephalosporins and related β-lactam compounds. These enzymes inactivate the antibiotics by hydrolysing the amide bond of the β-lactam ring. Class A β-lactamases are the most widespread enzymes and are responsible for numerous failures in the treatment of infectious diseases. The introduction of new β-lactam compounds, which are meant to be ‘β-lactamase-stable’ or β-lactamase inhibitors, is thus continuously challenged either by point mutations in the ubiquitous TEM and SHV plasmid-borne β-lactamase genes or by the acquisition of new genes coding for β-lactamases with different catalytic properties. On the basis of the X-ray crystallography structures of several class A β-lactamases, including that of the clinically relevant TEM-1 enzyme, it has become possible to analyse how particular structural changes in the enzyme structures might modify their catalytic properties. However, despite the many available kinetic, structural and mutagenesis data, the factors explaining the diversity of the specificity profiles of class A β-lactamases and their amazing catalytic efficiency have not been thoroughly elucidated. The detailed understanding of these phenomena constitutes the cornerstone for the design of future generations of antibiotics.
Skip Nav Destination
Follow us on Twitter @Biochem_Journal
Article navigation
March 1998
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Review Article|
March 01 1998
Catalytic properties of class A β-lactamases: efficiency and diversity Available to Purchase
André MATAGNE;
André MATAGNE
1
1Centre for Protein Engineering and Laboratoire d'Enzymologie, Université de Liège, Institut de Chimie B6, 4000 Liège (Sart Tilman), Belgium
1To whom correspondence should be addressed.
Search for other works by this author on:
Josette LAMOTTE-BRASSEUR;
Josette LAMOTTE-BRASSEUR
1Centre for Protein Engineering and Laboratoire d'Enzymologie, Université de Liège, Institut de Chimie B6, 4000 Liège (Sart Tilman), Belgium
Search for other works by this author on:
Jean-Marie FRÈRE
Jean-Marie FRÈRE
1Centre for Protein Engineering and Laboratoire d'Enzymologie, Université de Liège, Institut de Chimie B6, 4000 Liège (Sart Tilman), Belgium
Search for other works by this author on:
Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1998
1998
Biochem J (1998) 330 (2): 581–598.
Connected Content
A correction has been published:
Catalytic properties of class A β-lactamases: efficiency and diversity
Citation
André MATAGNE, Josette LAMOTTE-BRASSEUR, Jean-Marie FRÈRE; Catalytic properties of class A β-lactamases: efficiency and diversity. Biochem J 1 March 1998; 330 (2): 581–598. doi: https://doi.org/10.1042/bj3300581
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Follow us on Twitter @Biochem_Journal
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() View past webinars > |