5,6-dihydroorotate and cysteine

5,6-dihydroorotate has been researched along with cysteine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Björnberg, O; Jensen, KF; Larsen, S; Rowland, P	1
Björnberg, O; Jensen, KF; Jordan, DB; Palfey, BA	1

Other Studies

2 other study(ies) available for 5,6-dihydroorotate and cysteine

Article	Year
Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry, 1997, Dec-23, Volume: 36, Issue:51 Topics: Alkylating Agents; Binding Sites; Cysteine; Dihydroorotate Dehydrogenase; Dithionitrobenzoic Acid; Enzyme Inhibitors; Evolution, Molecular; Flavoproteins; Hydrogen-Ion Concentration; Kinetics; Lactococcus lactis; Mutagenesis, Site-Directed; Orotic Acid; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Spectrophotometry	1997
Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis. Archives of biochemistry and biophysics, 2001, Jul-15, Volume: 391, Issue:2 Topics: Binding Sites; Catalysis; Cysteine; Dihydroorotate Dehydrogenase; Escherichia coli; Fumarates; Lactobacillus; Mutation; Orotic Acid; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Recombinant Proteins; Serine; Substrate Specificity	2001

Article

Year

Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis.

Biochemistry, 1997, Dec-23, Volume: 36, Issue:51

Topics: Alkylating Agents; Binding Sites; Cysteine; Dihydroorotate Dehydrogenase; Dithionitrobenzoic Acid; Enzyme Inhibitors; Evolution, Molecular; Flavoproteins; Hydrogen-Ion Concentration; Kinetics; Lactococcus lactis; Mutagenesis, Site-Directed; Orotic Acid; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Spectrophotometry

1997

Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis.

Archives of biochemistry and biophysics, 2001, Jul-15, Volume: 391, Issue:2

Topics: Binding Sites; Catalysis; Cysteine; Dihydroorotate Dehydrogenase; Escherichia coli; Fumarates; Lactobacillus; Mutation; Orotic Acid; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Recombinant Proteins; Serine; Substrate Specificity

2001