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  2. Tryptophan (data page) - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_(data_page)

    ^a EINECS for Tryptophan ^a CID 9060 from PubChem ^a CID 6305 from PubChem This page was last edited on 12 April 2023, at 11:38 (UTC). Text is available ...

  3. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    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.

  4. Eosinophilia–myalgia syndrome - Wikipedia

    en.wikipedia.org/wiki/Eosinophilia–myalgia...

    Eosinophilia–myalgia syndrome is a rare, sometimes fatal neurological condition linked to the ingestion of the dietary supplement L-tryptophan. [1] [2] The risk of developing EMS increases with larger doses of tryptophan and increasing age. [3]

  5. α-Methyltryptophan - Wikipedia

    en.wikipedia.org/wiki/Α-Methyltryptophan

    [3] [4] [5] The preceding limitations of tryptophan make its use in PET imaging in humans impossible, whereas αMTP is a viable agent for such purposes. [ 5 ] αMTP is first converted by tryptophan hydroxylase into α-methyl-5-hydroxytryptophan (αM-5-HTP or α-methyl-5-HTP), the α-methylated analogue of 5-hydroxytryptophan (5-HTP), prior to ...

  6. Aromatic L-amino acid decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Aromatic_L-amino_acid_de...

    Aromatic L-amino acid decarboxylase is active as a homodimer. Before addition of the pyridoxal phosphate cofactor, the apoenzyme exists in an open conformation. Upon cofactor binding, a large structural transformation occurs as the subunits pull closer and close the active site. This conformational change results in the active, closed ...

  7. Kynurenine - Wikipedia

    en.wikipedia.org/wiki/Kynurenine

    l-Kynurenine is a metabolite of the amino acid l-tryptophan used in the production of niacin. Kynurenine is synthesized by the enzyme tryptophan dioxygenase , which is made primarily but not exclusively in the liver, and indoleamine 2,3-dioxygenase , which is made in many tissues in response to immune activation. [ 1 ]

  8. 5-Hydroxytryptophan - Wikipedia

    en.wikipedia.org/wiki/5-Hydroxytryptophan

    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]

  9. Tryptophan 2,3-dioxygenase - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_2,3-dioxygenase

    56720 Ensembl ENSG00000262635 ENSG00000151790 ENSMUSG00000028011 UniProt P48775 P48776 RefSeq (mRNA) NM_005651 NM_019911 RefSeq (protein) NP_005642 NP_064295 Location (UCSC) Chr 4: 155.85 – 155.92 Mb Chr 3: 81.86 – 81.88 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L ...

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