The Enzyme Database

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Accepted name: tyrosine transaminase
Reaction: L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
For diagram of reaction, click here, for mechanism, click here , for diagram of phenylalanine and tyrosine biosynthesis, click here and for diagram of the methionine-salvage pathway, click here
Other name(s): tyrosine aminotransferase; glutamic-hydroxyphenylpyruvic transaminase; glutamic phenylpyruvic aminotransferase; L-phenylalanine 2-oxoglutarate aminotransferase; L-tyrosine aminotransferase; phenylalanine aminotransferase; phenylalanine transaminase; phenylalanine-α-ketoglutarate transaminase; phenylpyruvate transaminase; phenylpyruvic acid transaminase; tyrosine-α-ketoglutarate aminotransferase; tyrosine-α-ketoglutarate transaminase; tyrosine-2-ketoglutarate aminotransferase; TyrAT
Systematic name: L-tyrosine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC (aspartate transaminase). The three isoenzymic forms are interconverted by EC (stem bromelain) and EC (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9014-55-5
1.  Canellakis, Z.N. and Cohen, P.P. Purification studies of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 53–62. [PMID: 13366978]
2.  Canellakis, Z.N. and Cohen, P.P. Kinetic and substrate specificity study of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 63–71. [PMID: 13366979]
3.  Jacoby, G.A. and La Ru, B.N. Studies on the specificity of tyrosine-α-ketoglutarate transaminase. J. Biol. Chem. 239 (1964) 419–424. [PMID: 14171223]
4.  Kenney, F.T. Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver. J. Biol. Chem. 234 (1959) 2707–2712. [PMID: 14408534]
5.  Miller, J.E. and Litwack, G. Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. J. Biol. Chem. 246 (1971) 3234–3240. [PMID: 4396841]
6.  Rowsell, E.V. Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues. Biochem. J. 64 (1956) 235–245. [PMID: 13363833]
7.  SentheShanmuganathan, S. The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae. Biochem. J. 77 (1960) 619–625. [PMID: 13750129]
8.  Heilbronn, J., Wilson, J. and Berger, B.J. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J. Bacteriol. 181 (1999) 1739–1747. [PMID: 10074065]
[EC created 1961]

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