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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.
Tryptophan hydroxylases catalyze the biopterin-dependent monooxygenation of tryptophan to 5-hydroxytryptophan (5-HTP), which is subsequently decarboxylated by aromatic amino acid decarboxylase to form the neurotransmitter serotonin (5-hydroxytryptamine or 5-HT). It is the rate-limiting enzyme in the biosynthesis of serotonin.
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 ...
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 synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan. [1] [2] It is commonly found in Eubacteria, [3] Archaebacteria, [4] Protista, [5] Fungi, [6] and Plantae. [7] However, it is absent from Animalia. [8] It is typically found as an α2β2 tetramer.
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]
Micrograph of paper autofluorescing under ultraviolet illumination. The individual fibres in this sample are around 10 μm in diameter.. Autofluorescence is the natural fluorescence of biological structures such as mitochondria and lysosomes, in contrast to fluorescence originating from artificially added fluorescent markers (fluorophores).
IAA is predominantly produced in cells of the apex and very young leaves of a plant. Plants can synthesize IAA by several independent biosynthetic pathways. Four of them start from tryptophan, but there is also a biosynthetic pathway independent of tryptophan. [2] Plants mainly produce IAA from tryptophan through indole-3-pyruvic acid.