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  2. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Tyrosine ball and stick model spinning. L-Tyrosine or tyrosine (symbol Tyr or Y) [2] or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a conditionally essential amino acid with a polar side group.

  3. List of human blood components - Wikipedia

    en.wikipedia.org/wiki/List_of_human_blood_components

    ~3.3 × 10 −1: per red blood cell ... 6.7-8.6 × 10 −8: Histidine: 9-17 × 10 −6: 1.1-3.8 × 10 −5: Hydrogen ion(pH 7.4) 4 ... 1.9-2.1 × 10 −1: 6.0-8.3 × ...

  4. Bruton's tyrosine kinase - Wikipedia

    en.wikipedia.org/wiki/Bruton's_tyrosine_kinase

    These domains include an amino terminal pleckstrin homology (PH) domain, a proline-rich TEC homology (TH) domain, SRC homology (SH) domains SH2 and SH3, as well as a protein kinase domain with tyrosine phosphorylation activity. [5] Part of the TH domain is folded against the PH domain while the rest is intrinsically disordered.

  5. Tyramine - Wikipedia

    en.wikipedia.org/wiki/Tyramine

    In foods, it often is produced by the decarboxylation of tyrosine during fermentation or decay. Foods that are fermented, cured, pickled, aged, or spoiled have high amounts of tyramine. Tyramine levels go up when foods are at room temperature or go past their freshness date. Specific foods containing considerable amounts of tyramine include: [6 ...

  6. Phenylalanine - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine

    It appears to cross the blood–brain barrier less efficiently than L-phenylalanine, and so a small amount of an ingested dose of D-phenylalanine is excreted in the urine without penetrating the central nervous system. [24] L-Phenylalanine is an antagonist at α 2 δ Ca 2+ calcium channels with a K i of 980 nM. [25]

  7. Tyrosine phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_phosphorylation

    Cartoon representation of the molecular structure of protein domain: p56 lck tyrosine kinase. Tyrosine phosphorylation is the addition of a phosphate (PO 4 3−) group to the amino acid tyrosine on a protein. It is one of the main types of protein phosphorylation. This transfer is made possible through enzymes called tyrosine kinases. Tyrosine ...

  8. Insulin receptor substrate 1 - Wikipedia

    en.wikipedia.org/wiki/Insulin_receptor_substrate_1

    3667 16367 Ensembl ENSG00000169047 ENSMUSG00000055980 UniProt P35568 P35569 RefSeq (mRNA) NM_005544 NM_010570 RefSeq (protein) NP_005535 NP_034700 Location (UCSC) Chr 2: 226.73 – 226.8 Mb Chr 1: 82.21 – 82.27 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Insulin receptor substrate 1 (IRS-1) is a signaling adapter protein that in humans is encoded by the IRS1 gene. It is a 180 ...

  9. Tyrosine aminotransferase - Wikipedia

    en.wikipedia.org/wiki/Tyrosine_aminotransferase

    In humans, the tyrosine aminotransferase protein is encoded by the TAT gene. [7] A deficiency of the enzyme in humans can result in what is known as type II tyrosinemia, wherein there is an abundance of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction to form 4-hydroxyphenylpyruvate. [8]