5,6-dihydroorotate has been researched along with flavin mononucleotide in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (80.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Jensen, KF; Mohsen, AW; Munro, AW; Rigby, SE; Scrutton, NS | 1 |
Basran, J; Combe, JP; Hothi, P; Leys, D; Munro, AW; Rigby, SE; Scrutton, NS | 1 |
Fagan, RL; Nelson, MN; Pagano, PM; Palfey, BA | 1 |
Al-Karadaghi, S; Dahlberg, L; Dufe, VT; Fritzson, I; Khairoullina, A; Svensson, B; Walse, B; Wellmar, U | 1 |
Alves, CN; Roitberg, AE; Silva, JR | 1 |
5 other study(ies) available for 5,6-dihydroorotate and flavin mononucleotide
Article | Year |
---|---|
Thermodynamic basis of electron transfer in dihydroorotate dehydrogenase B from Lactococcus lactis: analysis by potentiometry, EPR spectroscopy, and ENDOR spectroscopy.
Topics: Dihydroorotate Dehydrogenase; Dimerization; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Lactococcus lactis; NAD; Orotic Acid; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Potentiometry; Protein Subunits; Thermodynamics; Titrimetry | 2004 |
Lys-D48 is required for charge stabilization, rapid flavin reduction, and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis.
Topics: Catalysis; Dihydroorotate Dehydrogenase; Dimerization; Electrochemistry; Electron Transport; Flavin Mononucleotide; Flavins; Lactococcus lactis; Lysine; Mutagenesis, Site-Directed; NAD; Orotic Acid; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Protein Structure, Tertiary; Tyrosine | 2006 |
Mechanism of flavin reduction in class 2 dihydroorotate dehydrogenases.
Topics: Binding Sites; Catalysis; Dihydroorotate Dehydrogenase; Escherichia coli; Escherichia coli Proteins; Flavin Mononucleotide; Humans; Hydrogen-Ion Concentration; Models, Chemical; Orotic Acid; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Serine; Substrate Specificity | 2006 |
The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites.
Topics: Binding Sites; Biphenyl Compounds; Carboxylic Acids; Crystallography, X-Ray; Dihydroorotate Dehydrogenase; Enzyme Inhibitors; Flavin Mononucleotide; Humans; Naphthalenes; Orotic Acid; ortho-Aminobenzoates; Oxidoreductases Acting on CH-CH Group Donors; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Ubiquinone | 2008 |
Insights into the mechanism of oxidation of dihydroorotate to orotate catalysed by human class 2 dihydroorotate dehydrogenase: a QM/MM free energy study.
Topics: Binding Sites; Biocatalysis; Dihydroorotate Dehydrogenase; Flavin Mononucleotide; Humans; Molecular Dynamics Simulation; Orotic Acid; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Protein Structure, Tertiary; Quantum Theory; Thermodynamics | 2015 |