Article (Scientific journals)
The diversity, structure and regulation of beta-lactamases.
Philippon, A; Dusart, Jean; Joris, Bernard et al.
1998In Cellular and Molecular Life Sciences, 54 (4), p. 341-6
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Keywords :
Gene Expression Regulation, Bacterial; Gram-Negative Bacteria/enzymology/genetics; Gram-Positive Bacteria/enzymology/genetics; Models, Molecular; Serine/chemistry; Structure-Activity Relationship; Zinc/chemistry; beta-Lactamases/biosynthesis/chemistry/classification/metabolism
Abstract :
[en] beta-Lactamase production is responsible for the appearance of a large number of pathogenic bacterial strains exhibiting a high degree of resistance to beta-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 beta-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-beta-lactamases, but the detailed catalytic mechanisms might also differ widely, depending on the enzyme studied. Similarly, the induction of the synthesis of beta-lactamases is now better understood, but many questions remain to be answered.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Philippon, A
Dusart, Jean
Joris, Bernard ;  Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes
Frère, Jean-Marie ;  Université de Liège - ULiège > Centre d'ingénierie des protéines
Language :
English
Title :
The diversity, structure and regulation of beta-lactamases.
Publication date :
1998
Journal title :
Cellular and Molecular Life Sciences
ISSN :
1420-682X
eISSN :
1420-9071
Publisher :
Birkhäuser, Basel, Switzerland
Volume :
54
Issue :
4
Pages :
341-6
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 22 May 2012

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