Effect of alkaline pH on the activity of rat liver phenylalanine hydroxylase.

@article{Parniak1988EffectOA,
  title={Effect of alkaline pH on the activity of rat liver phenylalanine hydroxylase.},
  author={Michael A. Parniak and Michael Douglas Davis and Seymour. Kaufman},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 3},
  pages={
          1223-30
        }
}
The pH optimum of rat liver phenylalanine hydroxylase is dependent on the structure of the cofactor employed and on the state of activation of the enzyme. The tetrahydrobiopterin-dependent activity of native phenylalanine hydroxylase has a pH optimum of about 8.5. In contrast, the 6,7-dimethyltetrahydropterin-dependent activity is highest at pH 7.0. Activation of phenylalanine hydroxylase either by preincubation with phenylalanine or by limited proteolysis results in a shift of the pH optimum… CONTINUE READING

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Cold Spring Harbor Coni

J.-P. Abita, M. A. Parniak, S. Kaufman
  • Cell Proliferation
  • 1981

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