Article
Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35.
Antimicrobial agents and chemotherapy - 1 Apr 2016
Marcoccia Francesca, Bottoni Carlo, Sabatini Alessia, Colapietro Martina, Mercuri Paola Sandra, Galleni Moreno, Kerff Frédéric, Matagne André, Celenza Giuseppe, Amicosante Gianfranco, Perilli Mariagrazia
Abstract excerpt
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,...
Topics
- Amino Acid Substitution
- Anti-Bacterial Agents
- Biocatalysis
- Catalytic Domain
- Cephalosporins
- Cloning, Molecular
- Escherichia coli
- Gene Expression
- Isoleucine
- Kinetics
- Models, Molecular
- Mutation