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

Francesca Marcoccia | Zendy; Carlo Bottoni | Zendy; Alessia Sabatini | Zendy; Martina Colapietro | Zendy; Paola Sandra Mercuri | Zendy; Moreno Galleni | Zendy; Frédéric Kerff | Zendy; André Matagne | Zendy; Giuseppe Celenza | Zendy; Gianfranco Amicosante | Zendy; Mariagrazia Perilli | Zendy

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

Author(s) -

Francesca Marcoccia,

Carlo Bottoni,

Alessia Sabatini,

Martina Colapietro,

Paola Sandra Mercuri,

Moreno Galleni,

Frédéric Kerff,

André Matagne,

Giuseppe Celenza,

Gianfranco Amicosante,

Mariagrazia Perilli

Publication year - 2016

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.00531-15

Subject(s) - isoleucine , mutant , circular dichroism , enzyme , chemistry , threonine , stereochemistry , serine , biochemistry , wild type , amino acid , leucine , gene

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. Thekcat,Km, andkcat/Kmvalues calculated for the two mutants were slightly different from those of the wild-type enzyme. Interestingly, thekcat/Kmof 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.

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