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  Domain Name: arom_aa_hydroxylase
Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all homotetramers.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 41
Total Disease Mutations Found: 41
This domain occurred 4 times on human genes (9 proteins).



  ATTENTION DEFICIT-HYPERACTIVITY DISORDER, SUSCEPTIBILITY TO, 7
  HYPERPHENYLALANINEMIA, NON-PKU
  HYPERPHENYLALANINEMIA, NON-PKU MILD
  PHENYLKETONURIA
  PHENYLKETONURIA, INCLUDED
  SEGAWA SYNDROME, AUTOSOMAL RECESSIVE


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
metal binding site
cofactor binding site
















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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