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 reduction is observed for alpha-methylaspartate, which forms a stable, covalent external aldimine. The high population of...
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