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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 .
4.2 Blood or marrow ... signaling in promoting the growth of leukemic cells exhibiting the Ph chromosome and BCR-ABL tyrosine kinase activity. ... (q34.1;q11.2 ...
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.
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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 phosphorylation is a key step in signal transduction and the regulation of enzymatic activity.
1-2 × 10 −6: 1-2 × 10 −6: δ-Aminolevulinic acid: 1.5-2.3 × 10 −7: Ammonia nitrogen: 1-2 × 10 −6: 1.0-4.9 × 10 −7: cAMP: Intracellular signal transduction molecule male 5.6-10.9 × 10 −9: female 3.6-8.9 × 10 −9: Androstenedione: Steroid hormone: male >18 yrs 2-30 × 10 −10: female >18 yrs 8-30 × 10 −10: Androsterone ...
Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine.PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH 4, a pteridine cofactor) and a non-heme iron for catalysis.
Tyrosine hydroxylase or tyrosine 3-monooxygenase is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). [ 5 ] [ 6 ] It does so using molecular oxygen (O 2 ), as well as iron (Fe 2+ ) and tetrahydrobiopterin as cofactors .