Tirozin transaminaza

Tirozin transaminaza
Tirozin transaminaza dimer, E.Coli
Identifikatori
EC broj 2.6.1.5
CAS broj 9014-55-5
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Tirozin transaminaza (EC 2.6.1.5, tirozinska aminotransferaza, glutaminska-hidroksifenilpiruvinska transaminaza, glutaminska fenilpiruvinska aminotransferaza, L-fenilalanin 2-oksoglutaratna aminotransferaza, L-tirozinska aminotransferaza, fenilalaninska aminotransferaza, fenilalaninska transaminaza, fenilalanin-alfa-ketoglutaratna transaminaza, fenilpiruvatna transaminaza, fenilpiruvinsko kiselinska transaminaza, tirozin-alfa-ketoglutaratna aminotransferaza, tirozin-alfa-ketoglutaratna transaminaza, tirozin-2-ketoglutaratna aminotransferaza, TyrAT) je enzim sa sistematskim imenom L-tirozin:2-oksoglutarat aminotransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju

L-tirozin + 2-oksoglutarat 4-hidroksifenilpiruvat + L-glutamat

Ovaj enzim je piridoksal-fosfatni protein. L-fenilalanin može da deluje umesto L-tirozina.

Reference

  1. ↑ Canellakis, Z.N. and Cohen, P.P. (1956). „Purification studies of tyrosine-α-ketoglutaric acid transaminase”. J. Biol. Chem. 222: 53-62. PMID 13366978. 
  2. ↑ Canellakis, Z.N. and Cohen, P.P. (1956). „Kinetic and substrate specificity study of tyrosine-α-ketoglutaric acid transaminase”. J. Biol. Chem. 222: 63-71. PMID 13366979. 
  3. ↑ Jacoby, G.A. and La Ru, B.N. (1964). „Studies on the specificity of tyrosine-α-ketoglutarate transaminase”. J. Biol. Chem. 239: 419-424. PMID 14171223. 
  4. ↑ Kenney, F.T. (1959). „Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver”. J. Biol. Chem. 234: 2707-2712. PMID 14408534. 
  5. ↑ Miller, J.E. and Litwack, G. (1971). „Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase”. J. Biol. Chem. 246: 3234-3240. PMID 4396841. 
  6. ↑ Rowsell, E.V. (1956). „Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues”. Biochem. J. 64: 235-245. PMID 13363833. 
  7. ↑ SentheShanmuganathan, S. (1960). „The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae”. Biochem. J. 77: 619-625. PMID 13750129. 
  8. ↑ Heilbronn, J., Wilson, J. and Berger, B.J. (1999). „Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae”. J. Bacteriol. 181: 1739-1747. PMID 10074065. 

Literatura

Vanjske veze