Article
Variants of human dihydrofolate reductase with substitutions at leucine-22: effect on catalytic and inhibitor binding properties.
Molecular pharmacology - 1 Mar 1996
Ercikan-Abali E A, Waltham M C, Dicker A P, Schweitzer B I, Gritsman H, Banerjee D, Bertino J R
Abstract excerpt
We investigated the enzyme kinetic and antifolate inhibitory properties of human dihydrofolate reductase enzyme with mutations at position 22. Leu-22 was changed to isoleucine, methionine, phenylalanine, and tyrosine to generate the various mutant enzymes. The overall catalytic efficiency (kcat/K...
Topics
- Animals
- Base Sequence
- CHO Cells
- Cells, Cultured
- Cricetinae
- Enzyme Inhibitors
- Folic Acid Antagonists
- Genetic Variation
- Humans
- Isoleucine
- Kinetics
- Leucine
- Methotrexate
- Molecular Sequence Data
- Mutagenesis
- Mutation
- Structure-Activity Relationship
- Tetrahydrofolate Dehydrogenase