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The amino acid hydroxylases (monooxygenases), E.C.1.14.16.-, are iron-containing enzymes which utilise molecular oxygen and tetrahydrobiopterin as co-substrate and co-factor, respectively. In humans, as well as in other mammals, there are two distinct L-Tryptophan hydroxylase 2 genes. In humans, these genes are located on chromosomes 11 and 12 and encode two different homologous enzymes, TPH1 and TPH2.
Unless otherwise stated all data refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
L-Phenylalanine hydroxylase Show »
L-Tryptophan hydroxylase 1 Show »
L-Tryptophan hydroxylase 2 Show »
L-Tyrosine hydroxylase Show »
Further Reading Show »
Daubner, SC; Le, T; Wang, S. (2011) Tyrosine hydroxylase and regulation of dopamine synthesis. Arch. Biochem. Biophys., 508 (1): 1-12. [PMID:21176768]
Lehmann, IT; Bobrovskaya, L; Gordon, SL; Dunkley, PR; Dickson, PW. (2006) Differential regulation of the human tyrosine hydroxylase isoforms via hierarchical phosphorylation. J. Biol. Chem., 281 (26): 17644-51. [PMID:16644734]
Matthes, S; Mosienko, V; Bashammakh, S; Alenina, N; Bader, M. (2010) Tryptophan hydroxylase as novel target for the treatment of depressive disorders. Pharmacology, 85 (2): 95-109. [PMID:20130443]
Waider, J; Araragi, N; Gutknecht, L; Lesch, KP. (2011) Tryptophan hydroxylase-2 (TPH2) in disorders of cognitive control and emotion regulation: a perspective. Psychoneuroendocrinology, 36 (3): 393-405. [PMID:21257271]
Zhang, X; Beaulieu, JM; Gainetdinov, RR; Caron, MG. (2006) Functional polymorphisms of the brain serotonin synthesizing enzyme tryptophan hydroxylase-2. Cell. Mol. Life Sci., 63 (1): 6-11. [PMID:16378243]
References Show »
1. Greengard, O; Yoss, MS; Del Valle, JA. (1976) Alpha-methylphenylalanine, a new inducer of chronic hyperphenylalaninemia in sucling rats. Science, 192 (4243): 1007-8. [PMID:944951]
2. Nicholson, AN; Wright, CM. (1981) (+)-6-fluorotryptophan, an inhibitor of tryptophan hydroxylase: sleep and wakefulness in the rat. Neuropharmacology, 20 (4): 335-9. [PMID:6457252]