Reference : Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in comp...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78083
Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in complex with Enterobacter cloacae 908R beta-lactamase: evidence for a stereoselective mechanism from docking studies.
English
Michaux, Catherine [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Wouters, Johan [> > > >]
2005
Journal of the American Chemical Society
American Chemical Society
127
10
3262-3
Yes (verified by ORBi)
International
0002-7863
1520-5126
Washington
DC
[en] Crystallography, X-Ray ; Enterobacter cloacae/enzymology ; Lactams/chemistry/metabolism ; Models, Molecular ; Stereoisomerism ; Thermodynamics ; beta-Lactamases/chemistry/metabolism
[en] BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial beta-lactamases. The crystal structure of Enterobacter cloacae 908R class C beta-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C beta-lactamase.
http://hdl.handle.net/2268/78083
10.1021/ja0426241

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