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.
Site-directed mutagenesis of CphA indicated that prolines in the P158-P172 loop are essential for the stability and the catalytic activityof subclass B2 metallo--lactamases against carbapenems. The sequential substitution of proline led to a decrease of the catalytic effi-ciency of the variant compared to the wild-type (WT) enzyme but also to a higher affinity for the binding of the second zinc ion
Kinetic studies on CphA mutants reveal the role of the P158-P172 loop in activity versus carbapenems
BOTTONI, CARLO;PERILLI, MARIAGRAZIA;MARCOCCIA, FRANCESCA;Piccirilli, Alessandra;PELLEGRINI, CRISTINA;COLAPIETRO, MARTINA;SABATINI, ALESSIA;CELENZA, GIUSEPPE;AMICOSANTE, Gianfranco;
2016-01-01
Abstract
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.| File | Dimensione | Formato | |
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