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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.
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.
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.
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L-tyrosine + 2-oxoglutarate 4-hydroxyphenylpyruvate + L-glutamate 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 ...
Tyramine (/ ˈ t aɪ r ə m iː n / TY-rə-meen) (also spelled tyramin), also known under several other names, [note 1] is a naturally occurring trace amine derived from the amino acid tyrosine. [4] Tyramine acts as a catecholamine releasing agent .
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 .