Aspartat transaminaza
| Aspartat transaminaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.6.1.1 | ||||||||
| CAS broj | 9000-97-9 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aspartat transaminaza (EC 2.6.1.1, glutaminska-oksaloacetatna transaminaza, glutaminska-aspartinska transaminaza, transaminaza A, AAT, AspT, 2-oksoglutarat-glutamatna aminotransferaza, aspartat alfa-ketoglutaratna transaminaza, aspartatna aminotransferaza, aspartat-2-oksoglutaratna transaminaza, aspartinsko kiselinska aminotransferaza, aspartinska aminotransferaza, aspartilna aminotransferaza, AST, glutamat-oksalacetatna aminotransferaza, glutamat-oksalatna transaminaza, glutaminska-aspartinska aminotransferaza, glutaminska-oksalacetatna transaminaza, glutaminska oksalinska transaminaza, GOT (enzim), L-aspartatna transaminaza, L-aspartat-alfa-ketoglutaratna transaminaza, L-aspartat-2-ketoglutaratna aminotransferaza, L-aspartat-2-oksoglutaratna aminotransferaza, L-aspartat-2-oksoglutaratna transaminaza, L-aspartinska aminotransferaza, oksaloacetat-aspartatna aminotransferaza, oksaloacetatna transferaza, aspartat:2-oksoglutaratna aminotransferaza, glutamat oksaloacetatna transaminaza) je enzim sa sistematskim imenom L-aspartat:2-oksoglutarat aminotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- L-aspartat + 2-oksoglutarat oksaloacetat + L-glutamat
Ovaj enzim je piridoksal-fosfatni protein.
Reference
- ↑ Banks, B.E.C. and Vernon, C.A. (1961). „Transamination. Part I. The isolation of the apoenzyme of glutamic-aspartic transaminase from pig heart muscle”. J. Chem. Soc. (Lond.): 1698-1705.
- ↑ Bertland, L.H. and Kaplan, N.O. (1968). „Chicken heart soluble aspartate aminotransferase. Purification and properties”. Biochemistry 7: 134-142. PMID 5758538.
- ↑ Forest, J.C. and Wightman, F. (1973). „Amino acid metabolism in plants. III. Purification and some properties of a multispecific aminotransferase isolated from bushbean seedlings (Phaseolus vulgaris L.)”. Can. J. Biochem. 50: 813-829.
- ↑ Henson, C.P. and Cleland, W.W. (1964). „Kinetic studies of glutamic oxaloacetic transaminase isozymes”. Biochemistry 3: 338-345. PMID 14155095.
- ↑ Jenkins, W.T., Yphantis, D.A. and Sizer, I.W. (1959). „Glutamic aspartic transaminase. I. Assay, purification, and general properties”. J. Biol. Chem. 234: 51-57. PMID 13610891.
- ↑ Lowe, P.N. and Rowe, A.F. (1985). „Aspartate: 2-oxoglutarate aminotransferase from Trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase”. Biochem. J. 232: 689-695. PMID 3879173.
- ↑ Mavrides, C. and Orr, W. (1975). „Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli”. J. Biol. Chem. 250: 4128-4133. PMID 236311.
- ↑ Schreiber, G., Eckstein, M., Oeser, A. and Holzer, H. (1964). „[The concentration of aspartate aminotransferase from brewers’ yeast]”. Biochem. Z. 340: 13-20. PMID 14317947.
- ↑ Shrawder, E. and Martinez-Carrion, M. (1972). „Evidence of phenylalanine transaminase activity in the isoenzymes of aspartate transaminase”. J. Biol. Chem. 247: 2486-2492. PMID 4623131.
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.
Vanjske veze
- MeSH Aspartate+transaminase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
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
