Dihidroorotat dehidrogenaza (fumarat)
(Preusmjereno sa stranice DHODaza)
Dihidroorotat dehidrogenaza (fumarat) (EC 1.3.98.1, DHOdehaza (nespecifična), dihidroorotat dehidrogenaza (nespecifična), dihidoorotna kiselina dehidrogenaza (nespecifična), DHOD (nespecifična), DHODaza (nespecifična), dihidroorotatna oksidaza, pyr4 (gen)) je enzim sa sistematskim imenom (S)-dihidroorotat:fumarat oksidoreduktaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Dihidroorotat dehidrogenaza (fumarat) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 1.3.98.1 | ||||||||
| CAS broj | 2603876 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- (S)-dihidroorotat + fumarat orotat + sukcinat
Ovaj enzim vezuje FMN. Reakcija, koja se odvija u citozolu, je jedina redoks reakcija u de novo biosinteza pirimidinskih nukleotida.
Reference uredi
- ↑ Björnberg, O., Rowland, P., Larsen, S. and Jensen, K.F. (1997). „Active site of dihydroorotate dehydrogenase A from Lactococcus lactis' investigated by chemical modification and mutagenesis”. Biochemistry 36: 16197-16205. PMID 9405053.
- ↑ Rowland, P., Björnberg, O., Nielsen, F.S., Jensen, K.F. and Larsen, S. (1998). „The crystal structure of Lactococcus lactis' dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function”. Protein Sci. 7: 1269-1279. PMID 9655329.
- ↑ Nørager, S., Arent, S., Björnberg, O., Ottosen, M., Lo Leggio, L., Jensen, K.F. and Larsen, S. (2003). „Lactococcus lactis' dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function”. J. Biol. Chem. 278: 28812-28822. PMID 12732650.
- ↑ Zameitat, E., Pierik, A.J., Zocher, K. and Löffler, M. (2007). „Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues”. FEMS Yeast Res. 7: 897-904. PMID 17617217.
- ↑ Inaoka, D.K., Sakamoto, K., Shimizu, H., Shiba, T., Kurisu, G., Nara, T., Aoki, T., Kita, K. and Harada, S. (2008). „Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction”. Biochemistry 47: 10881-10891. PMID 18808149.
- ↑ Cheleski, J., Wiggers, H.J., Citadini, A.P., da Costa Filho, A.J., Nonato, M.C. and Montanari, C.A. (2010). „Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry”. Anal. Biochem. 399: 13-22. PMID 19932077.
Literatura uredi
- 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.