Article
Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase.
Biochemistry - 30 Jul 1991
Toney M D, Kirsch J F
Abstract excerpt
The aspartate aminotransferase mutant Y70F exhibits kcat = 8% and kcat/KM = 2% of the wild type values for the transamination of aspartate and alpha-ketoglutarate. The affinity of the enzyme for the noncovalently bound inhibitor maleate is reduced 17-fold by the mutation, while only a 2.5-fold re...
Topics
- Aspartate Aminotransferases
- Aspartic Acid
- Enzyme Inhibitors
- Escherichia coli
- Glutamates
- Glutamic Acid
- Isotopes
- Ketoglutaric Acids
- Kinetics
- Maleates
- Mutation
- N-Methylaspartate
- Spectrophotometry
- Tyrosine