Article

Cellular and Molecular Life Sciences CMLS

, Volume 54, Issue 4, pp 341-346

First online:

The diversity, structure and regulation of β-lactamases

  • A. PhilipponAffiliated withUniversité Paris VII, Hôpital Cochin, Service de Bactériologie, F-75475 Paris Cedex 14 (France)
  • , J. DusartAffiliated withCentre d’Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège (Belgium), Fax +32 4 366 3364, e-mail: jmfrere@ulg.ac.be
  • , B. JorisAffiliated withCentre d’Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège (Belgium), Fax +32 4 366 3364, e-mail: jmfrere@ulg.ac.be
  • , J.-M. FrèreAffiliated withCentre d’Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège (Belgium), Fax +32 4 366 3364, e-mail: jmfrere@ulg.ac.be

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Abstract.

β-Lactamase production is responsible for the appearance of a large number of pathogenic bacterial strains exhibiting a high degree of resistance to β-lactam antibiotics. A large number of enzymes have been described with very diverse primary structures and catalytic profiles. Nevertheless, all known three-dimensional structures of active-site serine β-lactamases exhibit a high degree of similarity with apparently equivalent chemical functionalities in the same strategic positions. These groups might not, however, play identical roles in the various classes of enzymes. Structural data have also been recently obtained for the zinc metallo-β-lactamases, but the detailed catalytic mechanisms might also differ widely, depending on the enzyme studied. Similarly, the induction of the synthesis of β-lactamases is now better understood, but many questions remain to be answered.

Key words.β-lactamases; penicillins; cephalosporins; regulation; classification.