Article
Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis.
Biochemistry - 5 Feb 1991
Beard W A, Appleman J R, Huang S M, Delcamp T J, Freisheim J H, Blakley R L
Abstract excerpt
The active sites of all bacterial and vertebrate dihydrofolate reductases that have been examined have a tryptophan residue near the binding sites for NADPH and dihydrofolate. In cases where the three-dimensional structure has been determined by X-ray crystallography, this conserved tryptophan residue makes hydrophobic and van der Waals interactions with the nicotinamide moiety of bound NADPH, and its indole...
Topics
- Allosteric Regulation
- Apoenzymes
- Binding Sites
- Humans
- Hydrogen
- Hydrogen-Ion Concentration
- Kinetics
- Ligands
- Mutation
- NADP
- Phenylalanine
- Protein Denaturation