Mutational Effects on Carbapenem Hydrolysis of YEM-1, a New Subclass B2 Metallo-β-Lactamase from Yersinia mollaretii

Author:

Mercuri Paola Sandra1,Esposito Roberto1,Blétard Sylvie1,Di Costanzo Stefano12,Perilli Mariagrazia2,Kerff Frédéric3,Galleni Moreno1

Affiliation:

1. Macromolécules Biologiques, Centre d’Ingénierie des Protéines, InBioS, Université de Liège, Liège, Belgium

2. Dipartimento di Scienze Cliniche Applicate e Biotecnologiche, Università degli Studi dell’Aquila, L’Aquila, Italy

3. Cristallographie des Macromolécules Biologiques, Centre d’Ingénierie des Protéines, InBioS, Université de Liège, Liège, Belgium

Abstract

Analysis of the genome sequence of Yersinia mollaretii ATCC 43969 identified the bla YEM gene, encoding YEM-1, a putative subclass B2 metallo-β-lactamase. The objectives of our work were to produce and purify YEM-1 and to complete its kinetic characterization. YEM-1 displayed the narrowest substrate range among known subclass B2 metallo-β-lactamases, since it can hydrolyze imipenem, but not other carbapenems, such as biapenem, meropenem, doripenem, and ertapenem, with high catalytic efficiency.

Funder

EU | Erasmus+

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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