Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35-Reference-Cited by-同舟云学术

Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35

Published:2016-04 Issue:4 Volume:60 Page:2366-2372
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Marcoccia Francesca¹,Bottoni Carlo¹,Sabatini Alessia¹,Colapietro Martina¹,Mercuri Paola Sandra²,Galleni Moreno²,Kerff Frédéric³,Matagne André⁴,Celenza Giuseppe¹,Amicosante Gianfranco¹,Perilli Mariagrazia¹

Affiliation:

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

2. Laboratoire de Macromolécules Biologiques, Centre d'Ingénierie des Protéines, Université de Liège, Liège, Belgium

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

4. Laboratoire d'Enzymologie et Repliement des Protéines, Centre d'Ingénierie des Protéines, Université de Liège, Liège, Belgium

Abstract

ABSTRACT Two laboratory mutants of NDM-1 were generated by replacing the isoleucine at position 35 with threonine and serine residues: the NDM-1 I35T and NDM-1 I35S enzymes. These mutants were well characterized, and their kinetic parameters were compared with those of the NDM-1 wild type. The k cat , K m , and k cat / K m values calculated for the two mutants were slightly different from those of the wild-type enzyme. Interestingly, the k cat / K m of NDM-1 I35S for loracarbef was about 14-fold higher than that of NDM-1. Far-UV circular dichroism (CD) spectra of NDM-1 and NDM-1 I35T and NDM-1 I35S enzymes suggest local structural rearrangements in the secondary structure with a marked reduction of α-helix content in the mutants.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.00531-15

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