tyrosine


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Related to tyrosine: tryptophan, Tyrosine hydroxylase, Tyrosine kinase

tyrosine

 [ti´ro-sēn]
a naturally occurring, nonessential amino acid present in most proteins and synthesized metabolically from phenylalanine. It is a precursor of melanin, catecholamines, and thyroid hormones.

ty·ro·sine (Tyr, Y),

(tī'rō-sēn, -sin),
2-Amino-3-(4-hydroxyphenyl)propionic acid; 3-(4-hydroxyphenyl)alanine; the l-isomer is an α-amino acid present in most proteins.

tyrosine

/ty·ro·sine/ (Tyr) (Y) (ti´ro-sēn) a naturally occurring, nonessential amino acid present in most proteins; it is a product of phenylalanine metabolism and a precursor of thyroid hormones, catecholamines, and melanin.

tyrosine

(tī′rə-sēn′)
n.
A nonessential amino acid, C9H11NO3, that is produced in the body from phenylalanine and is a precursor of melanin and of several neurotransmitters and hormones, such as epinephrine and thyroxine.

tyrosine (Tyr)

[tī′rəsēn]
Etymology: Gk, tyros
an amino acid synthesized in the body from the essential amino acid phenylalanine. Tyrosine is found in most proteins and is a precursor of melanin and several hormones, including epinephrine and thyroxine. See also amino acid, hormone, melanocyte.
enlarge picture
Chemical structure of tyrosine

ty·ro·sine

(Tyr, Y) (tī'rō-sēn)
An α-amino acid present in most proteins.

tyrosine

The AMINO ACID 4-hydroxyphenylalanine. This is one of the 20 amino acids that are incorporated into protein.
Tyrosineclick for a larger image
Fig. 308 Tyrosine . Molecular structure.

tyrosine (Y, Tyr)

one of the 20 AMINO ACIDS common in PROTEINS. It has a polar ‘R’ group structure and is soluble in water. See Fig. 308 . The ISOELECTRIC POINT of tyrosine is 5.7.

Tyrosine

A protein building block found in a wide variety of foods that is used by the body to make melanin.
Mentioned in: Albinism

tyrosine (tīˑ·r·sēn),

n an amino acid involved in the synthesis of neurotransmitters; has other functions. Has been used to treat sleep disorders, enhance cognitive function, and alleviate symptoms of ADD. No known precautions. Also called
L-tyrosine.
Enlarge picture
Chemical structure of tyrosine.

ty·ro·sine

(Tyr) (tī'rō-sēn)
An α-amino acid present in most proteins.

tyrosine (Tyr) (tī´rəsēn´),

n an amino acid synthesized in the body from the essential amino acid phenylalanine. Tyrosine is found in most proteins and is a precursor of melanin and several hormones, including epinephrine and thyroxine.

tyrosine, tyrosin

Tyr; a naturally occurring amino acid present in most proteins; it is a product of phenylalanine metabolism and a precursor of melanin, catecholamines and thyroid hormones.

tyrosine hydroxylase
an oxidase which converts tyrosine to dopa.
tyrosine tolerance test
used as a test of liver function but about 85% of liver parenchyma must be lost before the test gives a positive reaction.
References in periodicals archive ?
Pure tyrosine can increase the production of two neurotransmitters--dopamine and norepinephrine--as well as epinephrine, which is released from the adrenal gland when blood sugar falls too low or when you are under severe physical stress or acute, psychological stress that's great enough to raise your heart rate.
Time-dependent changes in protein tyrosine phosphorylation of guinea pig sperm during capacitation
A urine sample tested positive for SA and tyrosine metabolites at day 7, confirming the diagnosis of HT.
Instead, the cells had gone into overdrive, mass-producing Bcr-Abl tyrosine kinase.
Activated EGFR occurs in approximately 250,000 lung cancer patients worldwide, and the single T790M mutation accounts for over 50 percent of resistance to tyrosine kinase inhibitors in these patients who have limited treatment options available.
eNOS may also be phosphorylated at tyrosine residues, although the functional consequence of the enzyme is less clear.
The primers used to amplify tyrosine hydroxylase were designed to be mRNA-specific.
Some effects of transition metal and metal ions on the level of tyrosine phosphorylation of proteins in antigen-activated mast cells were observed (Figure 4).
Over the past few decades, Groffen and other researchers gradually deciphered the molecular basis of the cancer, including the site of the mutation and the role of Bcr-Abl tyrosine kinase.
Most people with CML have a genetic mutation, called the Philadelphia chromosome, which causes the bone marrow to make an enzyme called tyrosine kinase.
du Pont de Nemours and Company (Wilmington, DE) has patented a novel tyrosine-inducible tyrosine ammonia lyase enzyme isolated from the yeast Trichosporon cutaneum.
We previously demonstrated that nickel can activate an intracellular pathway leading to cytoskeleton reorganization consequent to tyrosine phosphorylation of [p60.