Dihydroorotate dehydrogenase (quinone)

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Dihydroorotate dehydrogenase (quinone)
Identifiers
EC number 1.3.5.2
CAS number 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
Dihydroorotate dehydrogenase (quinone)
Identifiers
Symbol DHOD-2
InterPro IPR005719
Membranome 250

Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2, 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.

References[edit]

  1. ^ 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. 
  2. ^ 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. PMID 3733756. 
  3. ^ 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. 
  4. ^ 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. 
  5. ^ 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. 

External links[edit]