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tyrosine (tīˈrəsēn), organic compound, one of the 20 amino acids 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. 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 (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 and norepinephrine as well as of the thyroid hormones, including thyroxine. Melanin, 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.

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The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.



[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.)


The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.


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.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
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In this study, we provide the first evidence that suppressed tyrosine phosphorylation of NR2B ameliorates migraine attacks and hyperalgesia induced by chronic migraines.
Haq, Innovative Effect of Illite on Improved Microbiological Conversion of L- Tyrosine to L-dopa by Aspergilus oryzae ME2 under Acidic Conditions, Braz.
Gattermann et al., "Nilotinib (formerly AMN107), a highly selective BCR-ABL tyrosine kinase inhibitor, is effective in patients with Philadelphia chromosome-positive chronic myelogenous leukemia in chronic phase following imatinib resistance and intolerance," Blood, vol.
The recombinant proteins were assayed for tyrosine kinase activity of [[gamma]-[sup.32]P]ATP on the crude protein extracts or after immobilization to glutathione-Sepharose beads.
For example, a drug which blocks the excessive production of tyrosine hydroxylase in people with Clock mutation could be used to block drug craving.
We hypothesize that alkylphenols could play a role in crustacean molting, notably affecting sclerotization by interfering with tyrosine incorporation into the cuticle during shell hardening.
Quantitative analysis of the Millon positive compounds in the urine of our patient while on a hospital diet revealed that the daily outputs of 4-HPL, tyrosine, 4-HPP, and 4-HPA were approximately 1000 mg, 350 mg, 250 mg, and 150 mg, respectively.
The Wnt receptor CRD domain is also found in MuSK and related orphan receptor tyrosine kinases.
However, Engelman and colleagues discovered that although mutant KRAS activates ERK signaling in human KRAS mutant colorectal cancers, receptor tyrosine kinases control PI3K signaling.
Extracellular calcium is not necessary for capacitation and protein tyrosine phosphorylation in human (Leclerc et al., 1998) and ram sperm (Patricia Grasa et al., 2006).
[USPRwire, Fri Aug 23 2019] This report on the tyrosine kinase inhibitors market analyzes the current and future scenario of the global market.
Summary: This report on the tyrosine kinase inhibitors market analyzes the current and future scenario of the global market.