Article
The kinetic mechanism of wild-type and mutant mouse dihydrofolate reductases.
Biochemistry - 29 May 1990
Thillet J, Adams J A, Benkovic S J
Abstract excerpt
A kinetic mechanism is presented for mouse dihydrofolate reductase that predicts all the steady-state parameters and full time-course kinetics. This mechanism was derived from association and dissociation rate constants and pre-steady-state transients by using stopped-flow fluorescence and absorb...
Topics
- Animals
- Aspartic Acid
- Binding Sites
- Escherichia coli
- Folic Acid
- Glutamates
- Glutamic Acid
- Hydrogen-Ion Concentration
- Kinetics
- Mice
- Mutation
- Tetrahydrofolate Dehydrogenase
