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
| Dihydroorotate dehydrogenase (fumarate) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.98.1 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- (S)-dihydroorotate + fumarate orotate + succinate
This enzyme contains FMN.
References
edit- ^ Björnberg O, Rowland P, Larsen S, Jensen KF (December 1997). "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis". Biochemistry. 36 (51): 16197–205. doi:10.1021/bi971628y. PMID 9405053.
- ^ Rowland P, Björnberg O, Nielsen FS, Jensen KF, Larsen S (June 1998). "The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function". Protein Science. 7 (6): 1269–79. doi:10.1002/pro.5560070601. PMC 2144028. PMID 9655329.
- ^ Nørager S, Arent S, Björnberg O, Ottosen M, Lo Leggio L, Jensen KF, Larsen S (August 2003). "Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function". The Journal of Biological Chemistry. 278 (31): 28812–22. doi:10.1074/jbc.M303767200. PMID 12732650.
- ^ Zameitat E, Pierik AJ, Zocher K, Löffler M (September 2007). "Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues". FEMS Yeast Research. 7 (6): 897–904. doi:10.1111/j.1567-1364.2007.00275.x. PMID 17617217.
- ^ Inaoka DK, Sakamoto K, Shimizu H, Shiba T, Kurisu G, Nara T, Aoki T, Kita K, Harada S (October 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): 10881–91. doi:10.1021/bi800413r. PMID 18808149.
- ^ Cheleski J, Wiggers HJ, Citadini AP, da Costa Filho AJ, Nonato MC, Montanari CA (April 2010). "Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry". Analytical Biochemistry. 399 (1): 13–22. doi:10.1016/j.ab.2009.11.018. PMID 19932077.
External links
edit- Dihydroorotate+dehydrogenase+(fumarate) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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