Dihydroorotate dehydrogenase (quinone)

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Dihydroorotate dehydrogenase (quinone)
EC number
CAS number 59088-23-2
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Dihydroorotate dehydrogenase (quinone) (EC, dihydroorotate:ubiquinone oxidoreductase, (S)-dihydroorotate:(acceptor) oxidoreductase, (S)-dihydroorotate:acceptor oxidoreductase, DHOdehase (ambiguous), DHOD (ambiguous), DHODase (ambiguous), DHODH) is an enzyme with systematic name (S)-dihydroorotate:quinone oxidoreductase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(S)-dihydroorotate + a quinone orotate + a quinol

This Class 2 dihydroorotate dehydrogenase enzyme contains FMN.


  1. ^ Forman, H.J.; Kennedy, J. (1978). "Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme". Arch. Biochem. Biophys. 191 (1): 23–31. doi:10.1016/0003-9861(78)90063-2. PMID 216313. 
  2. ^ Hines, V.; Keys, L.D. III; Johnston, M. (1986). "Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase". J. Biol. Chem. 261 (24): 11386–11392. PMID 3733756. 
  3. ^ Bader, B.; Knecht, W.; Fries, M.; Löffler, M. (1998). "Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase". Protein Expr. Purif. 13 (3): 414–422. doi:10.1006/prep.1998.0925. PMID 9693067. 
  4. ^ Fagan, R.L.; Nelson, M.N.; Pagano, P.M.; Palfey, B.A. (2006). "Mechanism of flavin reduction in Class 2 dihydroorotate dehydrogenases". Biochemistry. 45 (50): 14926–14932. doi:10.1021/bi060919g. PMID 17154530. 
  5. ^ Björnberg, O; Grüner, A.C.; Roepstorff, P.; Jensen, K.F. (1999). "The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis". Biochemistry. 38: 2899–2908. doi:10.1021/bi982352c. PMID 10074342. 

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