Dihydroorotate dehydrogenase (fumarate)

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Dihydroorotate dehydrogenase (fumarate)
Identifiers
EC number 1.3.98.1
CAS number 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

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 orotate + succinate

This enzyme contains FMN.

References[edit]

  1. ^ Björnberg, O.; Rowland, P.; Larsen, S.; Jensen, K.F. (1997). "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis' investigated by chemical modification and mutagenesis". Biochemistry. 36 (51): 16197–16205. doi:10.1021/bi971628y. PMID 9405053. 
  2. ^ Rowland, P.; Björnberg, O.; Nielsen, F.S.; Jensen, K.F.; Larsen, S. (1998). "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. doi:10.1002/pro.5560070601. PMC 2144028Freely accessible. PMID 9655329. 
  3. ^ Nørager, S.; Arent, S.; Björnberg, O.; Ottosen, M.; Lo Leggio, L.; Jensen, K.F.; Larsen, S. (2003). "Lactococcus lactis' dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function". J. Biol. Chem. 278 (31): 28812–28822. doi:10.1074/jbc.M303767200. PMID 12732650. 
  4. ^ Zameitat, E.; Pierik, A.J.; Zocher, K.; Löffle, M. (2007). "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 (6): 897–904. doi:10.1111/j.1567-1364.2007.00275.x. PMID 17617217. 
  5. ^ Inaoka, D.K.; Sakamoto, K.; Shimizu, H.; Shiba, T.; Kurisu, G.; Nara, T.; Aoki, T.; Kita, K.; Harada, S. (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): 10881–10891. doi:10.1021/bi800413r. PMID 18808149. 
  6. ^ Cheleski, J.; Wiggers, H.J.; Citadini, A.P.; da Costa Filho, A.J.; Nonato, M.C.; Montanari, C.A. (2010). "Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry". Anal. Biochem. 399 (1): 13–22. doi:10.1016/j.ab.2009.11.018. PMID 19932077. 

External links[edit]