blaVIM-7

metallo-beta-lactamase

Overview

Mutations

Protein Change	Nucleotide Change	Mechanism	Organism	Resistance To	Database	Validation Status
H224Y	-	-	-	carbapenems	Reslit	Candidate
F218Y	-	-	-	carbapenems	Reslit	Candidate

Papers1

His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo-β-Lactamase VIM-7.

Mutations in the L3 loop (His224Y) and L1 loop (Phe218Y) enhance catalytic efficiency and thermostability of VIM-7.

Protein Change: H224Y, F218Y
Confers Resistance To: carbapenems
Validation Method: mutational analysis, enzyme kinetics, crystal structures, and thermostability
Source Database: Reslit