(Izocitrat dehidrogenaza (NADP+)) kinaza
| (izocitrat dehidrogenaza (NADP+)) kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.11.5 | ||||||||
| CAS broj | 83682-93-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
(izocitrat dehidrogenaza (NADP+)) kinaza (EC 2.7.11.5, (izocitratna dehidrogenaza (NADP+)) kinaza, ICDH kinaza/fosfataza, IDH kinaza, IDH kinaza/fosfataza, IDH-K/P, IDHK/P, izocitrat dehidrogenaza kinaza (fosforilacija), izocitrat dehidrogenaza kinaza/fosfataza, STK3) je enzim sa sistematskim imenom ATP:(izocitrat dehidrogenaza (NADP+)) fosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + [izocitrat dehidrogenaza (NADP+)] ADP + [izocitrat dehidrogenaza (NADP+)] fosfat
Ovaj enzim nema aktivirajuće jedinjenje, ali je specifičan za svoj supstrat.
Reference
- ↑ Wang, J.Y.J. and Koshland, D.E., Jr. (1982). „The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium”. Arch. Biochem. Biophys. 218: 59-67. PMID 6756316.
- ↑ Miller, S.P., Karschnia, E.J., Ikeda, T.P. and LaPorte, D.C. (1996). „Isocitrate dehydrogenase kinase/phosphatase. Kinetic characteristics of the wild-type and two mutant proteins”. J. Biol. Chem. 271: 19124-19128. PMID 8702587.
- ↑ Singh, S.K., Matsuno, K., LaPorte, D.C. and Banaszak, L.J. (2001). „Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase”. J. Biol. Chem. 276: 26154-26163. PMID 11290745.
- ↑ Oudot, C., Cortay, J.C., Blanchet, C., Laporte, D.C., Di Pietro, A., Cozzone, A.J. and Jault, J.M. (2001). „T'he "catalytic" triad of isocitrate dehydrogenase kinase/phosphatase from E. coli and its relationship with that found in eukaryotic protein kinases”. Biochemistry 40: 3047-3055. PMID 11258918.
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 (isocitrate+dehydrogenase+(NADP+))+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
