[en] Site-directed mutagenesis of CphA indicated that prolines in the P158-P172 loop are essential for the stability and the catalytic activity of subclass B2 metallo-beta-lactamases against carbapenems. The sequential substitution of proline led to a decrease of the catalytic efficiency of the variant compared to the wild-type (WT) enzyme but also to a higher affinity for the binding of the second zinc ion.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bottoni, Carlo
Perilli, Mariagrazia
Marcoccia, Francesca
Piccirilli, Alessandra
Pellegrini, Cristina
Colapietro, Martina
Sabatini, Alessia
Celenza, Giuseppe
Kerff, Frédéric ; Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Amicosante, Gianfranco
Galleni, Moreno ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
Mercuri, Paola ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
Language :
English
Title :
Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in Activity versus Carbapenems.
Publication date :
2016
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
60
Issue :
5
Pages :
3123-6
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2016, American Society for Microbiology. All Rights Reserved.
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