Biology:Dihydroorotate dehydrogenase (fumarate)

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Dihydroorotate dehydrogenase (fumarate)
Identifiers
EC number1.3.98.1
CAS number2603876
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] orotate + succinate

This enzyme contains FMN.

References

  1. "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis". Biochemistry 36 (51): 16197–205. December 1997. doi:10.1021/bi971628y. PMID 9405053. 
  2. "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. June 1998. doi:10.1002/pro.5560070601. PMID 9655329. 
  3. "Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function". The Journal of Biological Chemistry 278 (31): 28812–22. August 2003. doi:10.1074/jbc.M303767200. PMID 12732650. 
  4. "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. September 2007. doi:10.1111/j.1567-1364.2007.00275.x. PMID 17617217. 
  5. "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. October 2008. doi:10.1021/bi800413r. PMID 18808149. 
  6. "Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry". Analytical Biochemistry 399 (1): 13–22. April 2010. doi:10.1016/j.ab.2009.11.018. PMID 19932077. 

External links