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

Carlo Bottoni | Zendy; Mariagrazia Perilli | Zendy; Francesca Marcoccia | Zendy; Alessandra Piccirilli | Zendy; Cristina Pellegrini | Zendy; Martina Colapietro | Zendy; Alessia Sabatini | Zendy; Giuseppe Celenza | Zendy; Frédéric Kerff | Zendy; Gianfranco Amicosante | Zendy; Moreno Galleni | Zendy; Paola Sandra Mercuri | Zendy

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

Author(s) -

Carlo Bottoni,

Mariagrazia Perilli,

Francesca Marcoccia,

Alessandra Piccirilli,

Cristina Pellegrini,

Martina Colapietro,

Alessia Sabatini,

Giuseppe Celenza,

Frédéric Kerff,

Gianfranco Amicosante,

Moreno Galleni,

Paola Sandra Mercuri

Publication year - 2016

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01703-15

Subject(s) - mutant , mutagenesis , proline , chemistry , enzyme , site directed mutagenesis , catalytic efficiency , catalysis , stereochemistry , saturated mutagenesis , biochemistry , biology , amino acid , gene

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-β-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.

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