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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.
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]
Serotonin and tryptophan have been found in chocolate with varying cocoa contents. The highest serotonin content (2.93 μg/g) was found in chocolate with 85% cocoa, and the highest tryptophan content (13.27–13.34 μg/g) was found in 70–85% cocoa. The intermediate in the synthesis from tryptophan to serotonin, 5-hydroxytryptophan, was not found.
Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin. Tyrosine hydroxylase , phenylalanine hydroxylase , and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases .
A common example of an indolamine is the tryptophan derivative serotonin, a neurotransmitter involved in mood and sleep. [1] Another example of an indolamine is melatonin . In biochemistry , indolamines are substituted indole compounds that contain an amino group.
L-Tryptophan to tryptamine – a trace amine neuromodulator; 5-HTP to serotonin (5-hydroxytryptamine) – a neurotransmitter; However, some of these reactions do not seem to bear much or any biological significance. For example, histamine is biosynthesised strictly via the enzyme histidine decarboxylase in humans and other organisms. [10] [11]
Examples are dopamine, norepinephrine and serotonin. All monoamines are derived from aromatic amino acids like phenylalanine, tyrosine, and tryptophan by the action of aromatic amino acid decarboxylase enzymes. They are deactivated in the body by the enzymes known as monoamine oxidases which clip off the amine group.
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]