Aspartat kinaza
| Aspartat kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Aspartat kinaza homodimer, Arabidopsis thaliana | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.2.4 | ||||||||
| CAS broj | 9012-50-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Aspartat kinaza (EC 2.7.2.4, aspartokinaza, AK, beta-aspartokinaza, aspartinska kinaza) je enzim sa sistematskim imenom ATP:L-aspartat 4-fosfotransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + L-aspartat ADP + 4-fosfo-L-aspartat
Enzim iz Escherichia coli je multifunkcionalni protein, koji takođe katalizuje reakciju EC 1.1.1.3, homoserin dehidrogenaze.
Reference
- ↑ Black, S. (1962). „Conversion of aspartic acid to homoserine”. Methods Enzymol. 5: 820-827.
- ↑ Paulus, H. and Gray, E. (1967). „Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. I. Kinetic studies”. J. Biol. Chem. 242: 4980-4986. PMID 6058940.
- ↑ Starnes, W.L., Munk, P., Maul, S.B., Cunningham, G.N., Cox, D.J. and Shive, W. (1972). „Threonine-sensitive aspartokinase-homoserine dehydrogenase complex, amino acid composition, molecular weight, and subunit composition of the complex”. Biochemistry 11: 677-687. PMID 4551091.
- ↑ Véron, M., Falcoz-Kelly, F. and Cohen, G.N. (1972). „The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain”. Eur. J. Biochem. 28: 520-527. PMID 4562990.
- ↑ Chassagnole, C., Rais, B., Quentin, E., Fell, D. A. and Mazat, J.-P. (2001). „An integrated study of threonine-pathway enzyme kinetics in Escherichia coli”. Biochem. J. 356: 415-423.
- ↑ Curien, G., Ravanel, S., Robert, M. and Dumas, R. (2005). „Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms”. J. Biol. Chem. 280: 41178-41183.
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+kinase
- 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
