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Catalytic properties of class A β-lactamases: efficiency and diversity
Author(s) -
André Matagne,
Josette LamotteBrasseur,
JeanMarie Frère
Publication year - 1998
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bj3310975v
Subject(s) - class (philosophy) , catalysis , diversity (politics) , catalytic efficiency , biology , computational biology , chemistry , combinatorial chemistry , evolutionary biology , computer science , biochemistry , artificial intelligence , political science , law
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-lactamasestable ’ 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.

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