Dihydroorotate dehydrogenase (fumarate)
| Dihydroorotate dehydrogenase (fumarate) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.3.98.1 | ||||||||
| CAS number | 2603876 | ||||||||
| 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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Dihydroorotate dehydrogenase (fumarate) (EC 1.3.98.1, dihydroorotate oxidase, pyr4 (gene)) is an enzyme with systematic name (S)-dihydroorotate:fumarate oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- (S)-dihydroorotate + fumarate orotate + succinate
This enzyme contains FMN.
References
- ↑ Björnberg, O.; Rowland, P.; Larsen, S.; Jensen, K.F. (1997). "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis' investigated by chemical modification and mutagenesis". Biochemistry. 36 (51): 16197–16205. doi:10.1021/bi971628y. PMID 9405053.
- ↑ Rowland, P.; Björnberg, O.; Nielsen, F.S.; Jensen, K.F.; 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. doi:10.1002/pro.5560070601. PMC 2144028
. PMID 9655329. - ↑ Nørager, S.; Arent, S.; Björnberg, O.; Ottosen, M.; Lo Leggio, L.; Jensen, K.F.; Larsen, S. (2003). "Lactococcus lactis' dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function". J. Biol. Chem. 278 (31): 28812–28822. doi:10.1074/jbc.M303767200. PMID 12732650.
- ↑ Zameitat, E.; Pierik, A.J.; Zocher, K.; Löffle, 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 (6): 897–904. doi:10.1111/j.1567-1364.2007.00275.x. PMID 17617217.
- ↑ Inaoka, D.K.; Sakamoto, K.; Shimizu, H.; Shiba, T.; Kurisu, G.; Nara, T.; Aoki, T.; Kita, K.; 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 (41): 10881–10891. doi:10.1021/bi800413r. PMID 18808149.
- ↑ Cheleski, J.; Wiggers, H.J.; Citadini, A.P.; da Costa Filho, A.J.; Nonato, M.C.; Montanari, C.A. (2010). "Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry". Anal. Biochem. 399 (1): 13–22. doi:10.1016/j.ab.2009.11.018. PMID 19932077.
External links
- Dihydroorotate dehydrogenase (fumarate) at the US National Library of Medicine Medical Subject Headings (MeSH)
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