Reference : Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/9387
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis
English
Bebrone, Carine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Anne, C. [> > > >]
De Vriendt, K. [> > > >]
Devreese, B. [> > > >]
Rossolini, G. M. [> > > >]
Van Beeumen, Jos [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
5-Aug-2005
Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc
280
31
28195-28202
Yes (verified by ORBi)
International
0021-9258
Bethesda
[en] Among class B beta-lactamases, the subclass B2 CphA enzyme is characterized by a unique specificity profile. CphA efficiently hydrolyzes only carbapenems. In this work, we generated site-directed mutants that possess a strongly broadened activity spectrum when compared with the WT CphA. Strikingly, the N116H/N220G double mutant exhibits a substrate profile close to that observed for the broad spectrum subclass B1 enzymes. The double mutant is significantly activated by the binding of a second zinc ion under conditions where the WT enzyme is non-competitively inhibited by the same ion.
http://hdl.handle.net/2268/9387
10.1074/jbc.M414052200
http://www.jbc.org/
The authors acknowledge the Biochemical Journal and the American Society for Biochemistry and Molecular Biology.

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