Article
How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases.
Biochemistry - 1 May 1990
Blacklow S C, Knowles J R
Abstract excerpt
The reaction energetics of four triosephosphate isomerase mutants are compared with those of the wild-type enzyme. The two primary mutants, E165D and H95N, contain site-specific alterations of active site residues. In one case the active site base has been altered (E165D), and in the other, an active site electrophile has been removed (H95N), yet the major effect in each case is the relative destabilization of...
Topics
- Animals
- Binding Sites
- Carbohydrate Epimerases
- Catalysis
- Dihydroxyacetone Phosphate
- Energy Transfer
- Glyceraldehyde 3-Phosphate
- Kinetics
- Mutation
- Structure-Activity Relationship
- Substrate Specificity