Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.3.5.2

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Composite Reactions Electron-Transfer-Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.3.5.2

Supersedes EC number: 1.3.99.11

Reaction Locations: inner membrane (sensu Gram-negative Bacteria)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: dihydroorotate dehydrogenase (quinone)

Enzyme Commission Synonyms: dihydroorotate:ubiquinone oxidoreductase, (S)-dihydroorotate:(acceptor) oxidoreductase, (S)-dihydroorotate:acceptor oxidoreductase, DHOdehase (ambiguous), DHOD (ambiguous), DHODase (ambiguous), DHODH

Enzyme Commission Summary:
This Class 2 dihydroorotate dehydrogenase enzyme contains FMN [Fagan06]. The enzyme is found in eukaryotes in the mitochondrial membrane and in some Gram negative bacteria associated with the cytoplasmic membrane [Hines86, Bjornberg99]. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides [Hines86, Fagan06]. The best quinone electron acceptors for the enzyme from bovine liver are coenzymes ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor but at lower rates [Hines86]. Methyl-, ethyl-, tert-butyl and benzyl-(S)-dihydroorotates are also substrates, but 1- and 3-methyl and 1,3-dimethyl methyl-(S)-dihydroorotates are not [[Hines86]. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor.

Citations: [Forman78, Bader98]

Unification Links: KEGG:R01868 , Rhea:18073

Relationship Links: BRENDA:EC:1.3.5.2 , ENZYME:EC:1.3.5.2 , IUBMB-ExplorEnz:EC:1.3.5.2 , UniProt:RELATED-TO:O76140

Credits:
Revised 13-Jan-2011 by Caspi R , SRI International


References

Bader98: Bader B, Knecht W, Fries M, Loffler M (1998). "Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase." Protein Expr Purif 13(3);414-22. PMID: 9693067

Bjornberg99: Bjornberg O, Gruner AC, Roepstorff P, Jensen KF (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. PMID: 10074342

Fagan06: Fagan RL, Nelson MN, Pagano PM, Palfey BA (2006). "Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases." Biochemistry 45(50);14926-32. PMID: 17154530

Forman78: Forman HJ, Kennedy J (1978). "Mammalian dihydroorotate dehydrogenase: physical and catalytic properties of the primary enzyme." Arch Biochem Biophys 191(1);23-31. PMID: 216313

Hines86: Hines V, Keys LD, Johnston M (1986). "Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase." J Biol Chem 261(24);11386-92. PMID: 3733756


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc13.