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: the role of the loop P158-P170 on the activity versus carbapenems

Perilli M;Piccirilli A;Pellegrini C;Celenza G;Amicosante G;
2016

Abstract

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
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11697/180373
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