(Piruvat dehidrogenaza (acetil-transfer)) kinaza
| (piruvat dehidrogenaza (acetil-transfer)) kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.11.2 | ||||||||
| CAS broj | 2620256 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
(piruvat dehidrogenaza (acetil-transfer)) kinaza (EC 2.7.11.2, PDH kinaza, PDHK, PDK, PDK1, PDK2, PDK3, PDK4, piruvatna dehidrogenaza kinaza, piruvat dehidrogenaza kinaza (fosforilacija), piruvat dehidrogenaza kinaza activator protein, STK1) je enzim sa sistematskim imenom ATP:(piruvat dehidrogenaza (acetil-transfer)) fosfotransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + [piruvat dehidrogenaza (acetil-transfer)] ADP + [piruvat dehidrogenaza (acetil-transfer)] fosfat
Ovaj enzim nema aktivirajuće jedinjenje, ali je specifičan za svoj supstrat.
Reference
- ↑ Linn, T.C., Pelley, J.W., Petit, F.H., Hucho, F., Randall, D.D. and Reed, L.J. (1972). „α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart”. Arch. Biochem. Biophys. 148: 327-342. PMID 4401694.
- ↑ Reed, L.J., Damuni, Z. and Merryfield, M.L. (1985). „Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation”. Curr. Top. Cell. Regul. 27: 41-49. PMID 3004826.
- ↑ Tovar-Mendez, A., Hirani, T.A., Miernyk, J.A. and Randall, D.D. (2005). „Analysis of the catalytic mechanism of pyruvate dehydrogenase kinase”. Arch. Biochem. Biophys. 434: 159-168. PMID 15629119.
- ↑ Bao, H., Kasten, S.A., Yan, X., Hiromasa, Y. and Roche, T.E. (2004). „Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP”. Biochemistry 43: 13442-13451. PMID 15491151.
- ↑ Roche, T.E., Hiromasa, Y., Turkan, A., Gong, X., Peng, T., Yan, X., Kasten, S.A., Bao, H. and Dong, J. (2003). „Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1”. Eur. J. Biochem. 270: 1050-1056. PMID 12631265.
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 (pyruvate+dehydrogenase+(acetyl-transferring))+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
