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Tyrosine aminotransferase information


Tyrosine transaminase
Human tyrosine aminotransferase (rainbow colored, N-terminus = blue, C-terminus = red) complexed with pyridoxal phosphate (space-filling model).[1]
Identifiers
EC no.2.6.1.5
CAS no.9014-55-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
TAT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTAT, Tat, tyrosine aminotransferase
External IDsOMIM: 613018 MGI: 98487 HomoloGene: 37293 GeneCards: TAT
EC number2.6.1.5
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000353

NM_146214

RefSeq (protein)

NP_000344

NP_666326

Location (UCSC)Chr 16: 71.57 – 71.58 MbChr 8: 110.72 – 110.73 Mb
PubMed search[4][5]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate.[6]

L-tyrosine + 2-oxoglutarate 4-hydroxyphenylpyruvate + L-glutamate

In humans, the tyrosine aminotransferase protein is encoded by the TAT gene.[7] A deficiency of the enzyme in humans can result in what is known as type II tyrosinemia, wherein there is an abundance of tyrosine as a result of tyrosine failing to undergo an aminotransferase reaction to form 4-hydroxyphenylpyruvate.[8]

  1. ^ PDB: 3DYD​; Karlberg T, Moche M, Andersson J, et al. (2008). "Human tyrosine aminotransferase". Protein Data Bank. doi:10.2210/pdb3dyd/pdb.
  2. ^ a b c GRCh38: Ensembl release 89: ENSG00000198650 – Ensembl, May 2017
  3. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001670 – Ensembl, May 2017
  4. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  6. ^ Dietrich JB (April 1992). "Tyrosine aminotransferase: a transaminase among others?". Cellular and Molecular Biology. 38 (2): 95–114. PMID 1349265.
  7. ^ Zea-Rey AV, Cruz-Camino H, Vazquez-Cantu DL, Gutiérrez-García VM, Santos-Guzmán J, Cantú-Reyna C (27 November 2017). "The Incidence of Transient Neonatal Tyrosinemia Within a Mexican Population". Journal of Inborn Errors of Metabolism and Screening. 5: 232640981774423. doi:10.1177/2326409817744230.
  8. ^ Rettenmeier R, Natt E, Zentgraf H, Scherer G (July 1990). "Isolation and characterization of the human tyrosine aminotransferase gene". Nucleic Acids Res. 18 (13): 3853–61. doi:10.1093/nar/18.13.3853. PMC 331086. PMID 1973834.

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Tyrosine aminotransferase

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Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate...

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by a deficiency of the enzyme tyrosine aminotransferase (EC 2.6.1.5), encoded by the gene TAT. Tyrosine aminotransferase is the first in a series of five...

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Tyrosinemia

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TAT gene, which encodes the enzyme tyrosine aminotransferase. As a result of TAT deficiency, the substrate tyrosine accumulates, causing ophthalmologic...

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Tat

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protein export pathway Tyrosine aminotransferase, an enzyme encoded by the TAT gene TAT, a codon for the amino acid Tyrosine Talbot railway station,...

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Diiodotyrosine transaminase

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5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase. Other names in common use include diiodotyrosine aminotransferase, halogenated tyrosine aminotransferase, and...

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Cathepsin T

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following chemical reaction: Interconversion of the three forms of tyrosine aminotransferase, EC 2.6.1.5. This enzyme degrades azocasein and denatured hemoglobin...

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Direct linear plot

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experimental errors are reasonably small, as in Fig. 1b of a study of tyrosine aminotransferase with seven observations, the lines crowd closely enough together...

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Glucocorticoid

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phosphatase) Increased gluconeogenesis – glucose 6-phosphatase and tyrosine aminotransferase The opposite mechanism is called transcriptional repression, or...

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Methionine transaminase

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L-methionine. Heilbronn J, Wilson J, Berger BJ (March 1999). "Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella...

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Alcohol and cancer

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May 2008. Retrieved 29 June 2009. "Oculocutaneous tyrosinemia/tyrosine aminotransferase deficiency". Atlas of Inherited Metabolic Diseases (3rd ed.)....

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Fumarylacetoacetate hydrolase

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expressed in the liver. FAH is among the amino acid hydroxylases. Tyrosine aminotransferase (TAT), 4-hydroxyphenylpyruvate dioxygenase (HPD), homogentisate...

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Dihydroxyphenylalanine transaminase

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aminotransferase. Other names in common use include dopa transaminase, dihydroxyphenylalanine aminotransferase, aspartate-DOPP transaminase...

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Nitinol biocompatibility

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In vitro tests use indicators of thrombosis, such as platelet, Tyrosine aminotransferase, and β-TG levels. Surface treatments that have to some extent...

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Arogenic acid

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aromatic-amino-acid transaminase, aspartate—prephenate aminotransferase and glutamate—prephenate aminotransferase: prephenate + amino acid → arogenate + keto acid...

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Amino acid synthesis

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acid, usually glutamate. The enzyme involved in this reaction is an aminotransferase. α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate Glutamate itself...

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Deborah Swackhamer

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Ribière, C.; Rouach, H.; Nordmann, R.; Nordmann, J. (1976-05-01). "Tyrosine aminotransferase activity in liver of pyrazole-treated rats". FEBS Letters. 64...

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Pyridoxal phosphate

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aldimine) with the ε-amino group of a specific lysine group of the aminotransferase enzyme. The α-amino group of the amino acid substrate displaces the...

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International Working Group on Neurotransmitter Related Disorders

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3-phosphoglycerate dehydrogenase, 3-phosphoserine phosphatase, phosphoserine aminotransferase, the glycine cleavage system (the deficiency is called glycine encephalopathy...

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from glutamate to another alpha-keto acid. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate...

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standard counterparts. Phosphorylation often occurs to serine, threonine, and tyrosine and involves replacing a hydrogen on the alcohol group at the terminus...

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