Effects of mutations in tyrosine hydroxylase associated with progressive dystonia on the activity and stability of the protein

@article{Royo2005EffectsOM,
  title={Effects of mutations in tyrosine hydroxylase associated with progressive dystonia on the activity and stability of the protein},
  author={Montserrat Royo and Susan Colette Daubner and Paul F. Fitzpatrick},
  journal={Proteins: Structure},
  year={2005},
  volume={58}
}
Tyrosine hydroxylase (TyrH) catalyzes the conversion of tyrosine to dihydroxyphenylalanine (DOPA), the rate‐limiting step in the biosynthesis of dopamine. Four mutations in the TyrH gene have recently been described in cases of autosomal recessive DOPA‐responsive dystonia (Swaans et al., Ann Hum Genet 2000;64:25–31). All four are predicted to result in changes in single amino acid residues in the catalytic domain of the protein: T245P, T283M, R306H, and T463M. To determine the effects of these… 
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TLDR
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TLDR
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Tyrosine hydroxylase (TyrH) is a pterin-dependent mononuclear non-heme aromatic amino acid hydroxylase that catalyzes the conversion of tyrosine to dihydroxyphenylalanine (DOPA). Chemical quench
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