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TPH

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Tryptophan hydroxylase

Tryptophan hydroxylase (TPH) (tryptophan 5-monooxygenase, EC 1.14.16.4) catalyses the reaction between tryptophan, 5,6,7,8-tetrahydrobiopterin (BH4) and O2 to give 5-hydroxytryptophan and 4a-hydroxy-tetrahydrobiopterin (4a-hydroxy-BH4. This reaction is the first and rate limiting step in the biosynthesis of serotonin (See scheme).

Together with phenylalanine hydroxylase (EC 1.14.16.1) and tyrosine hydroxylase (EC 1.14.16.2), TPH form the small enzyme family of aromatic amino acid hydroxylases (AAAH) []. These enzymes all contain iron and use BH4 as a co-substrate in the hydroxylation of their respective aromatic amino acids [ , , ]. Additionally all mammalian AAAH form homotetramers and each monomer consists of three domains. These domains are the N-terminal regulatory domain (100-150 residues), the catalytic domain (approximately 315 residues) and the C-terminal tetramerisation domain (approximately 30-40 residues) [ , , , ].


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Michael Skovbo Windahl, OCA

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