EC 1.3.98.1 - Dihydroorotate oxidase (fumarate)

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IntEnz Enzyme Nomenclature
EC 1.3.98.1

Names

Accepted name:
dihydroorotate oxidase (fumarate)
Other names:
DHODase [ambiguous]
DHOD [ambiguous]
DHOdehase [ambiguous]
dihydoorotic acid dehydrogenase [ambiguous]
dihydroorotate dehydrogenase [ambiguous]
dihydroorotate oxidase
pyr4 (gene name)
Systematic name:
(S)-dihydroorotate:fumarate oxidoreductase

Reaction

Cofactor

Comments:

Binds FMN. The reaction, which takes place in the cytosol, is the only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. Molecular oxygen can replace fumarate in vitro. Other class 1 dihydroorotate dehydrogenases use either NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. The membrane bound class 2 dihydroorotate dehydrogenase (EC 1.3.5.2) uses quinone as electron acceptor.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00708
Structural data: CSA , EC2PDB
Gene Ontology: GO:1990663 , GO:0052888
UniProtKB/Swiss-Prot: (40) [show] [UniProt]

References

  1. Björnberg, O., Rowland, P., Larsen, S., Jensen, K. F.
    Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis.
    Biochemistry 36: 16197-16205 (1997). [PMID: 9405053]
  2. Rowland, P., Bjornberg, O., Nielsen, F. S., Jensen, K. F., Larsen, S.
    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 (1998). [PMID: 9655329]
  3. Nørager, S., Arent, S., Björnberg, O., Ottosen, M., Lo Leggio, L., Jensen, K. F., Larsen, S.
    Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function.
    J. Biol. Chem. 278: 28812-28822 (2003). [PMID: 12732650]
  4. Zameitat, E., Pierik, A. J., Zocher, K., Loffler, M.
    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: 897-904 (2007). [PMID: 17617217]
  5. Inaoka, D. K., Sakamoto, K., Shimizu, H., Shiba, T., Kurisu, G., Nara, T., Aoki, T., Kita, K., Harada, S.
    Structures of Trypanosoma cruzi dihydroorotate dehydrogenase complexed with substrates and products: atomic resolution insights into mechanisms of dihydroorotate oxidation and fumarate reduction.
    Biochemistry 47: 10881-10891 (2008). [PMID: 18808149]
  6. Cheleski, J., Wiggers, H. J., Citadini, A. P., da Costa Filho, A. J., Nonato, M. C., Montanari, C. A.
    Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry.
    Anal. Biochem. 399: 13-22 (2010). [PMID: 19932077]

[EC 1.3.98.1 created 1961 as EC 1.3.3.1, transferred 2011 to EC 1.3.98.1]