Article
Site-saturation mutagenesis and three-dimensional modelling of ROB-1 define a substrate binding role of Ser130 in class A beta-lactamases.
Protein engineering - 1 Oct 1992
Juteau J M, Billings E, Knox J R, Levesque R C
Abstract excerpt
Site-saturation mutagenesis was performed on the class A ROB-1 beta-lactamase at conserved Ser130, which is centrally located in the antibiotic binding site where it can participate in both protein-protein and protein-substrate hydrogen bonding. Mutation Thr130 gave a beta-lactamase hydrolysing penicillins and cephalosporins but which showed a 3-fold lower affinity (Km) for ampicillin and cephalexin, and a...
Topics
- Ampicillin
- Base Sequence
- Binding Sites
- Cephalexin
- Computer Simulation
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Phenotype
- Protein Conformation
