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Phenylalanine Hydroxylase

An Aromatic Alliance

The tyrosine synthesized by the action of phenylalanine hydroxylase is required for the synthesis of various neurotransmitters that act on the nervous system and also control key functions like respiration and heart rate. During the synthesis of these neurotransmitters, tyrosine is further hydroxylated by the enzyme tyrosine hydroxylase. Interestingly, phenylalanine hydroxylase (PDB entry 1pah, shown on the left) and tyrosine hydroxylase (PDB entry 2toh, shown on the right) are structurally and functionally very similar to each other and also to tryptophan hydroxylase (PDB entry 1mlw). The last enzyme acts on the related amino acid tryptophan. All three enzymes use an iron ion, function as tetramers and have similar domain architecture. Since phenylalanine, tyrosine and tryptophan all have aromatic ring structures, these hydroxylases are together called aromatic amino acid hydroxylases.

For more information on phenylalanine hydroxylase from a genomic perspective, see the Protein of the Month at the European Bioinformatics Institute.

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Last changed by: A.Honegger, 8/4/06