Article
Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH.
The Journal of biological chemistry - 5 Apr 1990
Appleman J R, Howell E E, Kraut J, Blakley R L
Abstract excerpt
The apoenzyme of wild-type (WT) dihydrofolate reductase (DHRF) from Escherichia coli exists in two conformational states, Et and Ew, which differ in affinity for NADPH and in kinetic competence. Dissociation constants for the binary complex of NADPH with the two conformers differ by over 100-fold...
Topics
- Aspartic Acid
- Binding Sites
- Enzyme Activation
- Escherichia coli
- Kinetics
- Lacticaseibacillus casei
- Mutation
- NADP
- Protein Conformation
- Streptococcus
- Structure-Activity Relationship
- Tetrahydrofolate Dehydrogenase