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| Dihydroorotate:quinone oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.5.2 | ||||||||
| CAS no. | 59088-23-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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Class 2 dihydroorotate dehydrogenases (DHOQO, EC 1.3.5.2) is an enzyme with systematic name (S)-dihydroorotate:quinone oxidoreductase.[1][2][3][4][5] This enzyme catalyses the electron transfer from dihydroorotate (electron donor) to a quinone (electron acceptor):
- (S)-dihydroorotate + quinone orotate + quinol
These enzymes differ from class 1 dihydroorotate dehydrogenases (DHODH) on the electron acceptor, on their structure, and on their cellular localization. Since the reaction catalyzed by DHOQOs is both part of the electron transport chain and the pyrimidine de novo synthesis, it has been explored as a possible target for cancer treatment, immunological disorders and bacterial/viral infections.[6][7][8]
- ^ Forman HJ, Kennedy J (November 1978). "Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme". Archives of Biochemistry and Biophysics. 191 (1): 23–31. doi:10.1016/0003-9861(78)90063-2. PMID 216313.
- ^ Hines V, Keys LD, Johnston M (August 1986). "Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase". The Journal of Biological Chemistry. 261 (24): 11386–92. doi:10.1016/S0021-9258(18)67396-X. PMID 3733756.
- ^ Bader B, Knecht W, Fries M, Löffler M (August 1998). "Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase". Protein Expression and Purification. 13 (3): 414–22. doi:10.1006/prep.1998.0925. PMID 9693067.
- ^ Fagan RL, Nelson MN, Pagano PM, Palfey BA (December 2006). "Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases". Biochemistry. 45 (50): 14926–32. doi:10.1021/bi060919g. PMID 17154530.
- ^ Björnberg O, Grüner AC, Roepstorff P, Jensen KF (March 1999). "The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis". Biochemistry. 38 (10): 2899–908. doi:10.1021/bi982352c. PMID 10074342.
- ^ J. Leban, D. Vitt, Human dihydroorotate dehydrogenase inhibitors, a novel approach for the treatment of autoimmune and inflammatory diseases, Arzneimittel-Forschung/Drug Res. (2011). https://doi.org/10.1055/s-0031-1296169
- ^ R.I. Christopherson, S.D. Lyons, P.K. Wilson, Inhibitors of de novo nucleotide biosynthesis as drugs, Acc. Chem. Res. (2002). https://doi.org/10.1021/ar0000509
- ^ M. Löffler, L.D. Fairbanks, E. Zameitat, A.M. Marinaki, H.A. Simmonds, Pyrimidine pathways in health and disease, Trends Mol. Med. (2005). https://doi.org/10.1016/j.molmed.2005.07.003