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tyrosine
(redirected from Tyrosine hydroxylase)

   Also found in: Dictionary/thesaurus, Medical, Acronyms, Wikipedia, Hutchinson 0.04 sec.
tyrosine (tī`rəsēn), organic compound, one of the 20 amino acids amino acid (əmē`nō)
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 commonly found in animal proteins. Only the l-stereoisomer appears in mammalian protein. It is not essential to the human diet, since it can be synthesized in the body from phenylalanine phenylalanine (fĕn'əlăl`ənēn'), organic compound, one of the 22 α- amino acids commonly found in animal proteins.
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. When the enzyme that catalyzes the transformation of phenylalanine to tyrosine is not active because of a hereditary defect, the serious disease known as phenylketonuria phenylketonuria (fĕn'əlkēt'ən
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 (PKU) results. Other defects in tyrosine metabolism include the rare hereditary disorder known as alkaptonuria, characterized by discharge of a urine which darkens on standing exposed to air. Tyrosine is a precursor of the adrenal hormones epinephrine epinephrine (ĕp'ənĕf`rīn), hormone important to the body's metabolism, also known as adrenaline.
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 and norepinephrine norepinephrine (nôr'ĕpīnĕf`rən)
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 as well as of the thyroid hormones, including thyroxine thyroxine (thīrŏk`sēn), substance secreted by the thyroid gland .
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. Melanin melanin (mĕl`ənĭn), water-insoluble polymer of various compounds derived from the amino acid tyrosine .
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, the skin and hair pigment, is also derived from this amino acid. Tyrosine residues in enzymes have frequently been shown to be associated with active sites. Modification of these residues with various chemicals often results in a change in the specificity of the enzyme toward its substrates or even in total destruction of its activity. In 1846 tyrosine was obtained as a product of the degradation of the protein casein (from cheese). It was synthesized in the laboratory in 1883, and its structure was thus determined.

tyrosine

One of the amino acids, not essential for humans unless they have the hereditary disorder phenylketonuria. It is the biochemical precursor of many important catecholamines. It is found in small amounts in most proteins, especially insulin and papain (found in papaya). It is used in biochemical research and as a dietary supplement.



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They contrasted the effects on cell viability, DNA synthesis associated with cell replication, and increased expression of enzyme markers that characterize cholinergic or catecholaminergic phenotypes: choline acetyltranferase (CHAT) and tyrosine hydroxylase (TH), respectively.
In test-tube studies, the scientists found that the phthalide compound blocks the action of an enzyme called tyrosine hydroxylase, which the body used to produce catecholamines.
The neurons generated from the hES-derived precursors also synthesized neurotransmitters and a subpopulation expressed tyrosine hydroxylase.
 
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