CphA突变体的动力学研究揭示了P158 - P172环在对碳青霉烯类药物活性中的作用。
Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in Activity versus Carbapenems.
作者信息
Bottoni Carlo, Perilli Mariagrazia, Marcoccia Francesca, Piccirilli Alessandra, Pellegrini Cristina, Colapietro Martina, Sabatini Alessia, Celenza Giuseppe, Kerff Frédéric, Amicosante Gianfranco, Galleni Moreno, Mercuri Paola Sandra
机构信息
Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Università degli Studi dell'Aquila, L'Aquila, Italy.
Macromolécules Biologiques, Centre d'Ingénierie des Protéines (CIP), Université de Liège, Institut de Chimie B6, Sart Tilman, Liège, Belgium.
出版信息
Antimicrob Agents Chemother. 2016 Apr 22;60(5):3123-6. doi: 10.1128/AAC.01703-15. Print 2016 May.
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.
摘要
CphA的定点诱变表明，P158 - P172环中的脯氨酸对于B2亚类金属β-内酰胺酶对碳青霉烯类的稳定性和催化活性至关重要。与野生型（WT）酶相比，脯氨酸的顺序取代导致变体的催化效率降低，但也导致对第二个锌离子结合的更高亲和力。
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