Reference : Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a d...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/143759
Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme.
English
Horsfall, Louise [Université de Liège - ULiège > > Centre d'Ingénierie des Protéines > >]
Izougarhane, Youssef [> >]
Lassaux, Patricia mailto [Université de Liège - ULiège > > Centre d'Ingénierie des Protéines > >]
Selevsek, Nathalie [> >]
Liénard, Benoit [> >]
Poirel, Laurent [> >]
Kupper, Michaël [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > > > >]
Hoffmann, Kurt [Rheinisch - Westfälische Technische Hochschule Aachen - RWTH > > > >]
Frère, Jean-Marie [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Galleni, Moreno [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Bebrone, Carine mailto [Université de Liège - ULiège > > Centre d'Ingénierie des Protéines > >]
Apr-2011
FEBS Journal
Blackwell Publishing
278(8)
1252-1263
Yes (verified by ORBi)
International
1742-464X
Oxford
United Kingdom
[en] The metallo-β-lactamase (MBL) GOB-1 was expressed via a T7 expression system in Escherichia coli BL21(DE3). The MBL was purified to homogeneity and shown to exhibit a broad substrate profile, hydrolyzing all the tested β-lactam compounds efficiently. The GOB enzymes are unique among MBLs due to the presence of a glutamine residue at position 116, a zinc-binding residue in all known class B1 and B3 MBL structures. Here we produced and studied the Q116A, Q116N and Q116H mutants. The substrate profiles were similar for each mutant, but with significantly reduced activity compared with that of the wild-type. In contrast to the Q116H enzyme, which bound two zinc ions just like the wild-type, only one zinc ion is present in Q116A and Q116N. These results suggest that the Q116 residue plays a role in the binding of the zinc ion in the QHH site.
Belgian Federal Government ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; European Research Training Network ; European Commission
http://hdl.handle.net/2268/143759
10.1111/j.1742-4658.2011.08046.x
http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2011.08046.x/abstract;jsessionid=DCCF66F8F3D551214047544F4A0D984E.d04t04
We acknowledge Wiley-Blackwell. The definitive version is available at www3.interscience.wiley.com

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