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TPH
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| - | ==Tryptophan hydroxylase==
| + | #REDIRECT [[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).
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| - | 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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| - | {{STRUCTURE_3cin | PDB=3cin | SCENE= }}
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Current revision
- REDIRECT Hydroxylase
