Reference : The diversity, structure and regulation of beta-lactamases.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/123125
The diversity, structure and regulation of beta-lactamases.
English
Philippon, A [> > > >]
Dusart, Jean [ > > ]
Joris, Bernard mailto [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines]
1998
Cellular and Molecular Life Sciences : CMLS
Birkhäuser
54
4
341-6
Yes (verified by ORBi)
International
1420-682X
1420-9071
Basel
Switzerland
[en] 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
[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.
http://hdl.handle.net/2268/123125

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Open access
Publi_BJ_85.pdfPublisher postprint461.65 kBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.