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5-HTP is produced from the amino acid tryptophan through the action of the enzyme tryptophan hydroxylase. Tryptophan hydroxylase is one of the biopterin-dependent aromatic amino acid hydroxylases. Production of 5-HTP is the rate-limiting step in 5-HT (serotonin) synthesis. 5-HTP is normally rapidly converted to 5-HT by amino acid decarboxylase. [1]
Patients typically have normal levels of 5-hydroxyindolacetic acid (5HIAA), low levels of homovanillic acid (HVA) and 3-methoxy-4-hydroxyphenylethylene glycol (MHPG), and a low HVA:5-HIAA ratio. [1] Upon finding a pattern of CSF abrormalities suggestive of the disease, the diagnosis may be confirmed by analysing the TH gene encoding the enzyme. [1]
Tryptophan hydroxylase (TPH; EC 1.14.16.4) is the rate-limiting enzyme in the synthesis of serotonin (5-hydroxytryptamine, or 5HT). 5HT is causally involved in numerous central nervous activities, and it has several functions in peripheral tissues, including the maintenance of vascular tone and gut motility.[supplied by OMIM] [7]
Analogously to phenylalanine hydroxylase and tyrosine hydroxylase, this enzyme uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH 4) and dioxygen as cofactors. [ 2 ] In humans, the stimulation of serotonin production by administration of tryptophan has an antidepressant effect [ 3 ] [ 4 ] and inhibition of tryptophan hydroxylase (e.g. by p ...
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There is evidence that blood tryptophan levels are unlikely to be altered by changing the diet, [27] [28] but consuming purified tryptophan increases the serotonin level in the brain, whereas eating foods containing tryptophan does not. [29] In 2001 a Cochrane review of the effect of 5-HTP and tryptophan on depression was published. The authors ...
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TPH1 was first discovered to support serotonin synthesis in 1988 by converting tryptophan into 5-hydroxytryptophan. [6] It was thought that there only was a single TPH gene until 2003. A second form was found in the mouse ( Tph2 ), rat and human brain ( TPH2 ) and the original TPH was then renamed to TPH1.