Reference : Inactivation of Aeromonas Hydrophila Metallo-Beta-Lactamase by Cephamycins and Moxalactam
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/17339
Inactivation of Aeromonas Hydrophila Metallo-Beta-Lactamase by Cephamycins and Moxalactam
English
Zervosen, Astrid mailto [Université de Liège - ULg > > Centre de recherches du cyclotron >]
Valladares, Maria Hernandez [> > > >]
Devreese, Bart [> > > >]
Prosperi-Meys, Christelle mailto [Université de Liège - ULg > Département de physique > Département de physique >]
Adolph, Hans-Werner [> > > >]
Mercuri, Paola mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Vanhove, Marc [> >]
Amicosante, Gianfranco [> > > >]
van Beeumen, Jozef [> > > >]
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 >]
Jul-2001
European Journal of Biochemistry
268
13
3840-50
Yes (verified by ORBi)
International
0014-2956
[en] metallo-beta-lactamase ; beta-lactam ; inactivation ; disulfide bond ; cefoxitin ; moxalactam
[en] Incubation of moxalactam and cefoxitin with the Aeromonas hydrophila metallo-beta-lactamase CphA leads to enzyme-catalyzed hydrolysis of both compounds and to irreversible inactivation of the enzyme by the reaction products. As shown by electrospray mass spectrometry, the inactivation of CphA by cefoxitin and moxalactam is accompanied by the formation of stable adducts with mass increases of 445 and 111 Da, respectively. The single thiol group of the inactivated enzyme is no longer titrable, and dithiothreitol treatment of the complexes partially restores the catalytic activity. The mechanism of inactivation by moxalactam was studied in detail. Hydrolysis of moxalactam is followed by elimination of the 3' leaving group (5-mercapto-1-methyltetrazole), which forms a disulfide bond with the cysteine residue of CphA located in the active site. Interestingly, this reaction is catalyzed by cacodylate.
Centre d'Ingénierie des Protéines - CIP
http://hdl.handle.net/2268/17339

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