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Tryptophan ball and stick model spinning. Tryptophan (symbol Trp or W) [3] is an α-amino acid that is used in the biosynthesis of proteins.Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent.
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 and the original TPH was then renamed to TPH1. [7]
Certain indole derivatives were important dyestuffs until the end of the 19th century. In the 1930s, interest in indole intensified when it became known that the indole substituent is present in many important alkaloids, known as indole alkaloids (e.g., tryptophan and auxins), and it remains an active area of research today. [9]
Serotonin, an endogenous amine, is a neurotransmitter derived from the amino acid tryptophan. Serotonin is involved in regulating mood, sleep, appetite, and sexuality. [9] The amines are transmitted locally or via the blood system. The exogenous amines are directly absorbed from food in the intestine. Alcohol can increase the absorption rate.
Aromatic amino acids often serve as the precursors to important biochemicals. Histidine is the precursor to histamine. Tryptophan is the precursor to 5-hydroxytryptophan and then serotonin, tryptamine, auxin, kynurenines, and melatonin. [6]
121278 216343 Ensembl ENSG00000139287 ENSMUSG00000006764 UniProt Q8IWU9 Q8CGV2 RefSeq (mRNA) NM_173353 NM_173391 RefSeq (protein) NP_775489 NP_775567 Location (UCSC) Chr 12: 71.94 – 72.19 Mb Chr 10: 114.91 – 115.02 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tryptophan hydroxylase 2 (TPH2) is an isozyme of tryptophan hydroxylase found in vertebrates. In humans, TPH2 is ...
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 .
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.