Tirozin transaminaza
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
| 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 | ||||||||
| |||||||||
Ovaj enzim je piridoksal-fosfatni protein. L-fenilalanin može da deluje umesto L-tirozina.
Reference
uredi- ↑ Canellakis, Z.N. and Cohen, P.P. (1956). „Purification studies of tyrosine-α-ketoglutaric acid transaminase”. J. Biol. Chem. 222: 53-62. PMID 13366978.
- ↑ 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.
- ↑ 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.
- ↑ Kenney, F.T. (1959). „Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver”. J. Biol. Chem. 234: 2707-2712. PMID 14408534.
- ↑ Miller, J.E. and Litwack, G. (1971). „Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase”. J. Biol. Chem. 246: 3234-3240. PMID 4396841.
- ↑ Rowsell, E.V. (1956). „Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues”. Biochem. J. 64: 235-245. PMID 13363833.
- ↑ SentheShanmuganathan, S. (1960). „The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae”. Biochem. J. 77: 619-625. PMID 13750129.
- ↑ 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
uredi- 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.