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(tī`rəsēn), organic compound, one of the 20 amino acidsamino acid
, any one of a class of simple organic compounds containing carbon, hydrogen, oxygen, nitrogen, and in certain cases sulfur. These compounds are the building blocks of proteins.
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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 phenylalaninephenylalanine
, organic compound, one of the 22 α-amino acids commonly found in animal proteins. Only the l-stereoisomer appears in mammalian protein.
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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 phenylketonuriaphenylketonuria
(PKU), inherited metabolic disorder caused by a deficiency in a specific enzyme (phenylalanine hydroxylase). The absence of this enzyme, a recessive trait, prevents the body from making use of phenylalanine, one of the amino acids in most protein-rich foods, and
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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 epinephrineepinephrine
, hormone important to the body's metabolism, also known as adrenaline. Epinephrine, a catecholamine, together with norepinephrine, is secreted principally by the medulla of the adrenal gland.
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 and norepinephrinenorepinephrine
, a neurotransmitter in the catecholamine family that mediates chemical communication in the sympathetic nervous system, a branch of the autonomic nervous system.
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 as well as of the thyroid hormones, including thyroxinethyroxine
, substance secreted by the thyroid gland. The hormone thyroxine forms by combining the amino acid tyrosine with iodine. Complexed to a protein, it is stored in the follicle stems between thyroid cells.
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. Melaninmelanin
, water-insoluble polymer of various compounds derived from the amino acid tyrosine. It is one of two pigments found in human skin and hair and adds brown to skin color; the other pigment is carotene, which contributes yellow coloring.
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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.



[β-(para-hydroxyphenyl)alanine; oxyphenylaminopropionic acid], an amino acid. Tyrosine exists in the form of optically active D-and L-forms and the racemic DL-form. L-tyrosine is a constituent of many proteins and peptides, such as casein, fibroin, keratin, and insulin. It is readily isolated from protein hydrolysates because of its poor solubility in water. Phosphate esters of L-tyrosine are also components of proteins.

Tyrosine is a replaceable amino acid that is formed in animals and humans by the enzymic oxidation of phenylalanine. Disruption of this process gives rise to a serious hereditary disease, phenylpyruvic oligophrenia. The oxidation of tyrosine by the enzyme tyrosinase is an important intermediate reaction in the biosynthesis

of melanins, norepinephrine, and epinephrine in humans. The iodinated derivatives of tyrosine—thyroxine and triiodothyronine—are thyroid hormones.

Tyrosine performs an important function as a precursor in the biosynthesis of alkaloids, such as morphine, codeine, and papaverine. The enzymic oxidation of L-tyrosine is used to obtain the drug L-dopa. The breakdown of tyrosine in the body, in which ascorbic acid plays a role, results in the formation of fumarte and acetoacetic acids, which are incorporated into the Krebs cycle in the form of acetyl coenzyme A.


Meister, A. Biokhimiia aminokislot. Moscow, 1961. (Translated from English.)
Lehninger, A. Biokhimiia. Moscow, 1974. (Translated from English.)



C9H11NO3 A phenolic alpha amino acid found in many proteins; a precursor of the hormones epinephrine, norepinephrine, thyroxine, and triiodothyronine, and of the black pigment melanin.
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Interestingly, the tyrosine concentration in the blood spot was only 54 [micro]mol/L (1st percentile on day 2 of life, 31.
The combination gene had mutated further to encode a Bcr-Abl tyrosine kinase that's impervious to STI-571, Sawyers says.
Ponatinib was designed to block the abnormal tyrosine kinase, BCR-ABL, which drives CML and Ph+ALL," said Timothy P.
1177] tyrosine residues of eNOS or Akt1 phosphorylation (data not shown).
The aim of the present study was to develop a quantitative reverse transcription-PCR (RT-PCR) method for tyrosine hydroxylase mRNA for the detection of neuroblastoma cells in blood and bone marrow at diagnosis and during therapy and to evaluate the usefulness of this method for early and sensitive detection of relapsing disease during follow-up.
AVL-292 is a novel, orally available, covalent drug that inhibits Bruton's tyrosine kinase (Btk).
Mast cell activation is regulated by a complex signal transduction process that is initiated by phosphorylation of multiple mast cell proteins on tyrosine residues (Benhamou et al.
The drug targets cancer cells because only they contain the rogue enzyme, called Bcr-Abl tyrosine kinase.