Tyrosine aminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate.[6]
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]
^PDB: 3DYD; Karlberg T, Moche M, Andersson J, et al. (2008). "Human tyrosine aminotransferase". Protein Data Bank. doi:10.2210/pdb3dyd/pdb.
^ abcGRCh38: Ensembl release 89: ENSG00000198650 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000001670 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Dietrich JB (April 1992). "Tyrosine aminotransferase: a transaminase among others?". Cellular and Molecular Biology. 38 (2): 95–114. PMID 1349265.
^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.
^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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Tyrosineaminotransferase (or tyrosine transaminase) is an enzyme present in the liver and catalyzes the conversion of tyrosine to 4-hydroxyphenylpyruvate...
by a deficiency of the enzyme tyrosineaminotransferase (EC 2.6.1.5), encoded by the gene TAT. Tyrosineaminotransferase is the first in a series of five...
TAT gene, which encodes the enzyme tyrosineaminotransferase. As a result of TAT deficiency, the substrate tyrosine accumulates, causing ophthalmologic...
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following chemical reaction: Interconversion of the three forms of tyrosineaminotransferase, EC 2.6.1.5. This enzyme degrades azocasein and denatured hemoglobin...
experimental errors are reasonably small, as in Fig. 1b of a study of tyrosineaminotransferase with seven observations, the lines crowd closely enough together...
phosphatase) Increased gluconeogenesis – glucose 6-phosphatase and tyrosineaminotransferase The opposite mechanism is called transcriptional repression, or...
L-methionine. Heilbronn J, Wilson J, Berger BJ (March 1999). "Tyrosineaminotransferase catalyzes the final step of methionine recycling in Klebsiella...
expressed in the liver. FAH is among the amino acid hydroxylases. Tyrosineaminotransferase (TAT), 4-hydroxyphenylpyruvate dioxygenase (HPD), homogentisate...
In vitro tests use indicators of thrombosis, such as platelet, Tyrosineaminotransferase, and β-TG levels. Surface treatments that have to some extent...
acid, usually glutamate. The enzyme involved in this reaction is an aminotransferase. α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate Glutamate itself...
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...
3-phosphoglycerate dehydrogenase, 3-phosphoserine phosphatase, phosphoserine aminotransferase, the glycine cleavage system (the deficiency is called glycine encephalopathy...
from glutamate to another alpha-keto acid. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate...
standard counterparts. Phosphorylation often occurs to serine, threonine, and tyrosine and involves replacing a hydrogen on the alcohol group at the terminus...
Pralsetinib is a tyrosine kinase inhibitor. It is taken by mouth. The most common adverse reactions include increased aspartate aminotransferase (AST), decreased...