Dihidroorotat dehidrogenaza (hinon)
| Dihidroorotat dehidrogenaza (hinon) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.3.5.2 | ||||||||
| CAS broj | 59088-23-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Dihidroorotat dehidrogenaza (hinon) (EC 1.3.5.2, dihidroorotat:ubihinon oksidoreduktaza, (S)-dihidroorotat:(akceptor) oksidoreduktaza, (S)-dihidroorotat:akceptor oksidoreduktaza, DHOdehaza (nespecifična), DHOD (nespecifična), DHODase (nespecifična), DHODH) je enzim sa sistematskim imenom (S)-dihidroorotat:hinon oksidoreduktaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
Ova dihidroorotatna dehidrogenaza klase 2 sadrži contains FMN. Enzim je prisutan kod eukariota u mitohondrijskoj membrani, i u pojedinim gram negativnim bakterijama vezan za ćelijsku membranu. Reakcija posredovana ovim enzimom je jedina redoks reakcija u de novo biosintezi pirimidinskih nukleotida. Najbolji hinonski elektronski akceptori za enzim iz goveđe jetre su ubihinon-6 i ubihinon-7, mada jednostavni hinoni, kao što je benzohinon, takođe mogu deluju kao manje efikasni akceptori.
Reference[uredi | uredi kod]
- ↑ Forman, H.J. and Kennedy, J. (1978). „Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme”. Arch. Biochem. Biophys. 191: 23-31. PMID 216313.
- ↑ Hines, V., Keys, L.D., III and Johnston, M. (1986). „Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase”. J. Biol. Chem. 261: 11386-11392. PMID 3733756.
- ↑ Bader, B., Knecht, W., Fries, M. and Löffler, M. (1998). „Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase”. Protein Expr. Purif. 13: 414-422. PMID 9693067.
- ↑ Fagan, R.L., Nelson, M.N., Pagano, P.M. and Palfey, B.A. (2006). „Mechanism of flavin reduction in Class 2 dihydroorotate dehydrogenases”. Biochemistry 45: 14926-14932. PMID 17154530.
- ↑ Björnberg, O., Grüner, A.C., Roepstorff, P. and Jensen, K.F. (1999). „The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis”. Biochemistry 38: 2899-2908. PMID 10074342.
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.