Ornitin aminotransferaza
| Ornitin aminotransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Dimer ornitin aminotransferaze (čovjek) | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.6.1.13 | ||||||||
| CAS broj | 9030-42-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Ornitin aminotransferaza (EC 2.6.1.13, ornitinska delta-transaminaza, L-ornitin:alfa-ketoglutarat delta-aminotransferaza, OAT, L-ornitin 5-aminotransferaza, L-ornitinska aminotransferaza, ornitinska 5-aminotransferaza, ornitinska transaminaza, ornitin-alfa-ketoglutaratna aminotransferaza, ornitin-2-oksokiselinska aminotransferaza, ornitin-keto kiselinska aminotransferaza, ornitin-keto kiselinska transaminaza, ornitin-ketoglutaratna aminotransferaza, ornitin-okso kiselinska aminotransferaza, ornitin:alfa-oksoglutarat transaminaza, ornitin---okso-kiselinska transaminaza) je enzim sa sistematskim imenom L-ornitin:2-okso-kiselina aminotransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-ornitin + 2-okso karboksilat L-glutamat 5-semialdehid + L-aminokiselina
Ovaj enzim je piridoksal-fosfatni protein.
Reference[uredi | uredi kod]
- ↑ Fincham, J.R.S. (1953). „Ornithine transaminase in Neurospora and its relation to the biosynthesis of proline”. Biochem. J. 53: 313-320. PMID 13032071.
- ↑ Katunuma, N., Matsuda, Y. and Tomino, I. (1964). „Studies on ornithine-ketoacid transaminase. I. Purification and properties”. J. Biochem. (Tokyo) 56: 499-503. PMID 14244051.
- ↑ Meister, A. (1954). „Enzymatic transamination reactions involving arginine and ornithine”. J. Biol. Chem. 206: 587-596. PMID 13143017.
- ↑ Peraino, C., Bunville, L.G. and Tahmisian, T.N. (1969). „Chemical, physical, and morphological properties of ornithine aminotransferase from rat liver”. J. Biol. Chem. 244: 2241-2249. PMID 5783831.
- ↑ Quastel, J.H. and Witty, R. (1951). „Ornithine transaminase”. Nature 167: 556-556. PMID 14826840.
- ↑ Strecker, H.J. (1965). „Purification and properties of rat liver ornithine δ-transaminase”. J. Biol. Chem. 240: 1225-1230. PMID 14284729.
Literatura[uredi | uredi kod]
- 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.