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, Jensen KF (December 1997). "Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis". Biochemistry. 36 (51): 16197–205. doi:10.1021/bi971628y. PMID 9405053.
^ Rowland P, Björnberg O, Nielsen FS, Jensen KF, Larsen S (June 1998). "The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function". Protein Science. 7 (6): 1269–79. doi:10.1002/pro.5560070601. PMC 2144028. PMID 9655329.
^ Nørager S, Arent S, Björnberg O, Ottosen M, Lo Leggio L, Jensen KF, Larsen S (August 2003). "Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function". The Journal of Biological Chemistry. 278 (31): 28812–22. doi:10.1074/jbc.M303767200. PMID 12732650.
^ Zameitat E, Pierik AJ, Zocher K, Löffler M (September 2007). "Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues". FEMS Yeast Research. 7 (6): 897–904. doi:10.1111/j.1567-1364.2007.00275.x. PMID 17617217.
^ Inaoka DK, Sakamoto K, Shimizu H, Shiba T, Kurisu G, Nara T, Aoki T, Kita K, Harada S (October 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): 10881–91. doi:10.1021/bi800413r. PMID 18808149.
^ Cheleski J, Wiggers HJ, Citadini AP, da Costa Filho AJ, Nonato MC, Montanari CA (April 2010). "Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry". Analytical Biochemistry. 399 (1): 13–22. doi:10.1016/j.ab.2009.11.018. PMID 19932077.

External links

Dihydroorotate+dehydrogenase+(fumarate) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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