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L-Tyrosine or tyrosine (symbol Tyr or Y) 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. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is encoded by the codons UAC and UAU in messenger RNA.
The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available. Note that T was assigned to the structurally simpler threonine, U was avoided for its similarity with V for valine, W was assigned to tryptophan, while X was reserved for undetermined or atypical amino acids. The mnemonic tYrosine was also proposed. |
Read full article at Wikipedia
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InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1 |
OUYCCCASQSFEME-QMMMGPOBSA-N |
N[C@@H](Cc1ccc(O)cc1)C(O)=O |
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Mus musculus
(NCBI:txid10090)
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Source: BioModels - MODEL1507180067
See:
PubMed
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Mycoplasma genitalium
(NCBI:txid2097)
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See:
PubMed
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Chlamydomonas reinhardtii
(NCBI:txid3055)
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See:
PubMed
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Saccharomyces cerevisiae
(NCBI:txid4932)
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Source: yeast.sf.net
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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Homo sapiens
(NCBI:txid9606)
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See:
DOI
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Homo sapiens
(NCBI:txid9606)
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Found in
blood serum
(BTO:0000133).
See:
MetaboLights Study
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Bronsted base
A molecular entity capable of accepting a hydron from a donor (Bronsted acid).
(via organic amino compound )
Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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micronutrient
Any nutrient required in small quantities by organisms throughout their life in order to orchestrate a range of physiological functions.
fundamental metabolite
Any metabolite produced by all living cells.
EC 1.3.1.43 (arogenate dehydrogenase) inhibitor
An EC 1.3.1.* (oxidoreductase acting on CH-CH group of donor, NAD+ or NADP+ as acceptor) inhibitor that interferes with the action of arogenate dehydrogenase (EC 1.3.1.43).
Daphnia magna metabolite
A Daphnia metabolite produced by the species Daphnia magna.
(via tyrosine )
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nutraceutical
A product in capsule, tablet or liquid form that provide essential nutrients, such as a vitamin, an essential mineral, a protein, an herb, or similar nutritional substance.
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View more via ChEBI Ontology
(−)-α-amino-p-hydroxyhydrocinnamic acid
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NIST Chemistry WebBook
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(2S)-2-amino-3-(4-hydroxyphenyl)propanoic acid
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IUPAC
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(S)-(-)-Tyrosine
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HMDB
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(S)-2-Amino-3-(p-hydroxyphenyl)propionic acid
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KEGG COMPOUND
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(S)-3-(p-Hydroxyphenyl)alanine
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KEGG COMPOUND
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(S)-α-amino-4-hydroxybenzenepropanoic acid
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NIST Chemistry WebBook
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(S)-Tyrosine
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HMDB
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4-hydroxy-L-phenylalanine
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NIST Chemistry WebBook
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L-Tyrosin
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ChEBI
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L-Tyrosine
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KEGG COMPOUND
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Tyr
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ChEBI
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TYROSINE
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PDBeChem
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Tyrosine
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KEGG COMPOUND
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Y
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ChEBI
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2786
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DrugCentral
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C00001397
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KNApSAcK
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C00082
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KEGG COMPOUND
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c0234
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UM-BBD
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D00022
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KEGG DRUG
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DB00135
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DrugBank
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ECMDB00158
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ECMDB
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HMDB0000158
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HMDB
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TYR
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MetaCyc
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TYR
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PDBeChem
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Tyrosine
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Wikipedia
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YMDB00364
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YMDB
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View more database links |
392441
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Reaxys Registry Number
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Reaxys
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50929
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Gmelin Registry Number
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Gmelin
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60-18-4
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CAS Registry Number
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KEGG COMPOUND
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60-18-4
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CAS Registry Number
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NIST Chemistry WebBook
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60-18-4
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CAS Registry Number
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ChemIDplus
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Liu X, Luo L, Ding Y, Kang Z, Ye D (2012) Simultaneous determination of L-cysteine and L-tyrosine using Au-nanoparticles/poly-eriochrome black T film modified glassy carbon electrode. Bioelectrochemistry (Amsterdam, Netherlands) 86, 38-45 [PubMed:22360849] [show Abstract] A novel Au-nanoparticles/poly-eriochrome black T film modified glassy carbon electrode (AuNPs/PEBT/GCE) was constructed for the simultaneous determination of l-cysteine (L-Cys) and l-tyrosine (L-Tyr) by differential pulse voltammetry. Fourier transform infrared spectra and electrochemical impedance spectroscopy indicate that the PEBT film was successfully polymerized on the surface of GCE and the film efficiently decreased the charge transfer resistance value of electrode and improved the electron transfer kinetic between analytes and electrode. The scanning electron microscope image shows that the immobilized AuNPs were spherical in shape and enhanced the electrical conductivity of PEBT film. In addition, PEBT film increased the oxidation currents of analytes four times when compared to bare GCE, and the AuNPs separated the oxidation potentials of L-Cys and L-Tyr by 488 mV while bare GCE failed to resolve them. The amperometry results exhibit that the electrocatalytic currents increased linearly with L-Cys concentrations in the range 0.05-100 μM (r=0.9981), and the detection limits of L-Cys and L-Tyr were 8 nM and 10 nM (S/N=3), respectively. With high sensitivity and selectivity, the proposed electrochemical sensor provides a simple method for simultaneous determination of L-Cys and L-Tyr. | Sa M, Ying L, Tang AG, Xiao LD, Ren YP (2012) Simultaneous determination of tyrosine, tryptophan and 5-hydroxytryptamine in serum of MDD patients by high performance liquid chromatography with fluorescence detection. Clinica chimica acta; international journal of clinical chemistry 413, 973-977 [PubMed:22402312] [show Abstract]
BackgroundTyrosine (Tyr), Tryptophan (Trp) and 5-hydroxytryptamine (5-HT) are important amino acids in vivo and have been hypothesized to be involved in many mental disorders. We developed a rapid and sensitive HPLC method for simultaneous measurement of serum Tyr, Trp and 5-HT and explored the clinical significances of Tyr, Trp and 5-HT and the 5-HT/Trp ratio for patients with major depressive disorder (MDD) disease.MethodsSerum samples were deproteinized by 5% perchloric acid and separated on an Atlantis C18 column (4.6 × 150 mm, 5 μm) with the mobile phase consisting of 0.1 mol/l KH(2)PO(4) and methanol (85:15, V/V).The eluates were monitored by the fluorescence detection with programmed wavelength.ResultsAnalysis was achieved in <12.0 min. The limits of quantification were 0.014, 0.005, and 0.024 μmol/l for Tyr, Trp and 5-HT, respectively. Reproducibility and recovery were satisfactory. Tyr, Trp and 5-HT and the 5-HT/Trp ratio were significantly decreased in patients with MDD.ConclusionsIn diseases, like MDD, Tyr, Trp and 5-HT play an important role. This method can potentially be applied as prognostic or diagnostic tool or even to follow the evolution of the illness or of the treatment. | Bonner CA, Jensen RA, Gander JE, Keyhani NO (2004) A core catalytic domain of the TyrA protein family: arogenate dehydrogenase from Synechocystis. The Biochemical journal 382, 279-291 [PubMed:15171683] [show Abstract] The TyrA protein family includes prephenate dehydrogenases, cyclohexadienyl dehydrogenases and TyrA(a)s (arogenate dehydrogenases). tyrA(a) from Synechocystis sp. PCC 6803, encoding a 30 kDa TyrA(a) protein, was cloned into an overexpression vector in Escherichia coli. TyrA(a) was then purified to apparent homogeneity and characterized. This protein is a model structure for a catalytic core domain in the TyrA superfamily, uncomplicated by allosteric or fused domains. Competitive inhibitors acting at the catalytic core of TyrA proteins are analogues of any accepted cyclohexadienyl substrate. The homodimeric enzyme was specific for L-arogenate (K(m)=331 microM) and NADP+ (K(m)=38 microM), being unable to substitute prephenate or NAD+ respectively. L-Tyrosine was a potent inhibitor of the enzyme (K(i)=70 microM). NADPH had no detectable ability to inhibit the reaction. Although the mechanism is probably steady-state random order, properties of 2',5'-ADP as an inhibitor suggest a high preference for L-arogenate binding first. Comparative enzymology established that both of the arogenate-pathway enzymes, prephenate aminotransferase and TyrA(a), were present in many diverse cyanobacteria and in a variety of eukaryotic red and green algae. |
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