Dihydroorotate dehydrogenase (fumarate)

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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

\rightleftharpoons

orotate + succinate

This enzyme contains FMN.

References

↑ Björnberg, O., Rowland, P., Larsen, S. and 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.
↑ Rowland, P., Björnberg, O., Nielsen, F.S., Jensen, K.F. and 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 2144028. PMID 9655329.
↑ Nørager, S., Arent, S., Björnberg, O., Ottosen, M., Lo Leggio, L., Jensen, K.F. and 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.
↑ Zameitat, E., Pierik, A.J., Zocher, K. and Löffler, 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.
↑ Inaoka, D.K., Sakamoto, K., Shimizu, H., Shiba, T., Kurisu, G., Nara, T., Aoki, T., Kita, K. and 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.
↑ Cheleski, J., Wiggers, H.J., Citadini, A.P., da Costa Filho, A.J., Nonato, M.C. and 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

Dihydroorotate dehydrogenase (fumarate) at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: CH–CH oxidoreductases (EC 1.3)

1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase

1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase

1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD

1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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