Compounds > glutamine

glutamine and dithionite

glutamine has been researched along with dithionite in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19903 (60.00)18.7374
1990's0 (0.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Geary, LE; Meister, A1
Lea, PJ; Miflin, BJ2
Curti, B; Dossena, L; Florencio, FJ; Martin-Figueroa, E; Mattevi, A; Morandi, P; Ravasio, S; Vanoni, MA1
Huang, HW; Inoue, M; Kataoka, K; Kitagawa, R; Naruse, D; Sakurai, T1

Other Studies

5 other study(ies) available for glutamine and dithionite

ArticleYear
On the mechanism of glutamine-dependent reductive amination of alpha-ketoglutarate catalyzed by glutamate synthase.
    The Journal of biological chemistry, 1977, May-25, Volume: 252, Issue:10

    Topics: Ammonia; Apoenzymes; Dithionite; Enterobacter; Enterobacteriaceae; Escherichia coli; Flavins; Glutamate Synthase; Glutamates; Glutaminase; Glutamine; Hydrogen-Ion Concentration; Iron; Ketoglutaric Acids; NADP; Transaminases; Water

1977
Glutamate synthase in blue-green algae.
    Biochemical Society transactions, 1975, Volume: 3, Issue:3

    Topics: Ammonia; Cyanobacteria; Dithionite; Ferredoxins; Glutamate Synthase; Glutamates; Glutamine; Ketoglutaric Acids; NAD; NADP; Nitrogen; Transaminases

1975
The occurrence of glutamate synthase in algae.
    Biochemical and biophysical research communications, 1975, Jan-02, Volume: 64, Issue:3

    Topics: Aminooxyacetic Acid; Cell-Free System; Chlorella; Dithionite; Glutamate Synthase; Glutamine; Ketoglutaric Acids; Transaminases

1975
Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.
    Biochemistry, 2002, Jun-25, Volume: 41, Issue:25

    Topics: Amino Acid Oxidoreductases; Azospirillum brasilense; Catalysis; Cyanobacteria; Dithionite; Ferredoxins; Glutamic Acid; Glutaminase; Glutamine; Ketoglutaric Acids; NADP; Oxidation-Reduction; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry; Sulfites; Tetrazolium Salts; Titrimetry

2002
Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen.
    Biochemistry, 2005, May-10, Volume: 44, Issue:18

    Topics: Alanine; Amino Acid Substitution; Asparagine; Aspartic Acid; Copper; Cysteine; Dithionite; Fungal Proteins; Glutamic Acid; Glutamine; Hypocreales; Ligands; Methionine; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Oxygen; Point Mutation; Protons; Serine

2005