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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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 ⇌ {\displaystyle \rightleftharpoons } 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

  • Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X. 
  • Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036. 
  • Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0. 
  • Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097. 
  • Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X. 
  • Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842. 

Spoljašnje veze

  • MeSH Tyrosine+transaminase
  • p
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TemeTipovi
EC1 Oksidoreduktaze/spisak  • EC2 Transferaze/spisak  • EC3 Hidrolaze/spisak  • EC4 Lijaze/spisak  • EC5 Izomeraze/spisak  • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6