| Literature DB >> 26883708 |
Carlo Bottoni1, Mariagrazia Perilli1, Francesca Marcoccia1, Alessandra Piccirilli1, Cristina Pellegrini1, Martina Colapietro1, Alessia Sabatini1, Giuseppe Celenza1, Frédéric Kerff2, Gianfranco Amicosante1, Moreno Galleni2, Paola Sandra Mercuri3.
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.Entities:
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Year: 2016 PMID: 26883708 PMCID: PMC4862501 DOI: 10.1128/AAC.01703-15
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191