Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in Activity versus Carbapenems.

[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 :

Issue :

Pages :

3123-6

Peer reviewed :

Peer Reviewed verified by ORBi

Commentary :

Available on ORBi :

since 05 July 2016

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Bibliography

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Bebrone C, Delbrück H, Kupper MB, Schlömer P, Willmann C, Frère JM, Fischer R, Galleni M, Hoffmann KM. 2009. The structure of the di-zinc subclass B2 metallo-β-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site. Antimicrob Agents Chemother 53:4464-4471. http://dx.doi.org/10.1128/AAC.00288-09.

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