EC 2.6.1.5 - Tyrosine transaminase

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IntEnz Enzyme Nomenclature
EC 2.6.1.5

Names

Accepted name:
tyrosine transaminase
Other names:
L-phenylalanine 2-oxoglutarate aminotransferase
L-tyrosine aminotransferase
glutamic phenylpyruvic aminotransferase
glutamic—hydroxyphenylpyruvic transaminase
phenylalanine aminotransferase
phenylalanine transaminase
phenylalanine—α-ketoglutarate transaminase
phenylpyruvate transaminase
phenylpyruvic acid transaminase
tyrosine aminotransferase
tyrosine—2-ketoglutarate aminotransferase
tyrosine—α-ketoglutarate aminotransferase
tyrosine—α-ketoglutarate transaminase
TyrAT
Systematic name:
L-tyrosine:2-oxoglutarate aminotransferase

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , DIAGRAM , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00098
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004838
CAS Registry Number: 9014-55-5
UniProtKB/Swiss-Prot: (14) [show] [UniProt]

References

  1. Canellakis, Z.N. and Cohen, P.P.
    Purification studies of tyrosine-α-ketoglutaric acid transaminase.
    J. Biol. Chem. 222 : 53-62 (1956). [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 : 63-71 (1956). [PMID: 13366979]
  3. Jacoby, G.A. and La Du, B.N.
    Studies on the specificity of tyrosine-α-ketoglutarate transaminase.
    J. Biol. Chem. 239 : 419-424 (1964). [PMID: 14171223]
  4. Kenney, F.T.
    Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver.
    J. Biol. Chem. 234 : 2707-2712 (1959). [PMID: 14408534]
  5. Miller, J.E. and Litwack, G.
    Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase.
    J. Biol. Chem. 246 : 3234-3240 (1971). [PMID: 4396841]
  6. Rowsell, E.V.
    Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues.
    Biochem. J. 64 : 235-245 (1956). [PMID: 13363833]
  7. SentheShanmuganathan, S.
    The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae.
    Biochem. J. 77 : 619-625 (1960). [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 : 1739-1747 (1999). [PMID: 10074065]

[EC 2.6.1.5 created 1961]