Reference : Three factors that modulate the activity of class D β-lactamases and interfere with t...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/74943
Three factors that modulate the activity of class D β-lactamases and interfere with the post-translational carboxylation of Lys 70
English
Vercheval, Lionel [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Di Paolo, Alexandre mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Borel, Franck [> >]
Ferrer, Jean-Luc [> >]
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Matagne, André mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
Kerff, Frédéric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
25-Nov-2010
Biochemical Journal
Portland Press
432
3
495-504
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] beta-lactamase ; chloride inhibition ; hydrophobic core ; Lysine carboxylatin ; post-translational modification
[en] Lys-70 carboxylation in the active site of class D β lactamases is essential for their activity. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val-117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D β lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys 70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl-enzyme is the rate limiting step for the wild type OXA 10 β lactamase.
Centre d'Ingénierie des Protéines - CIP
http://hdl.handle.net/2268/74943

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