Stepwise improvements in catalytic effectiveness: independence and interdependence in combinations of point mutations of a sluggish triosephosphate isomerase.

Abstract excerpt

Second-site suppressor changes that improve the catalytic potency of a sluggish mutant of the enzyme triosephosphate isomerase have been examined both individually and in combination. Each of the second-site mutations increases the specific catalytic activity of a triosephosphate isomerase in which the catalytic base, glutamate-165, has been changed to aspartate. These second-site suppressors are G10S, S96P,...

Topics

• Animals
• Binding Sites
• Catalysis
• Escherichia coli
• Kinetics
• Muscles
• Mutation
• Rabbits
• Suppression, Genetic
• Triose-Phosphate Isomerase