5-enolpyruvoylshikimate-3-phosphate has been researched along with flavin mononucleotide in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (50.00) | 18.2507 |
2000's | 3 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bornemann, S; Lowe, DJ; Macheroux, P; Petersen, J; Thorneley, RN | 1 |
Bornemann, S; Ghisla, S; Macheroux, P; Thorneley, RN | 1 |
Bornemann, S; Koch, MH; Macheroux, P; Schönbrunn, E; Svergun, DI; Thorneley, RN; Volkov, VV | 1 |
Abell, C; Bornemann, S; Osborne, A; Thorneley, RN | 1 |
Amrhein, N; Kitzing, K; Macheroux, P | 1 |
Bornemann, S; Ehammer, H; Macheroux, P; Rauch, G | 1 |
6 other study(ies) available for 5-enolpyruvoylshikimate-3-phosphate and flavin mononucleotide
Article | Year |
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Binding of the oxidized, reduced, and radical flavin species to chorismate synthase. An investigation by spectrophotometry, fluorimetry, and electron paramagnetic resonance and electron nuclear double resonance spectroscopy.
Topics: Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Fluorometry; Free Radicals; Light; Lyases; Magnetic Resonance Spectroscopy; Organophosphorus Compounds; Oxidation-Reduction; Phosphorus-Oxygen Lyases; Shikimic Acid | 1996 |
Studies with flavin analogs provide evidence that a protonated reduced FMN is the substrate-induced transient intermediate in the reaction of Escherichia coli chorismate synthase.
Topics: Enzyme Inhibitors; Escherichia coli; Flavin Mononucleotide; Lyases; Organophosphorus Compounds; Phosphorus-Oxygen Lyases; Shikimic Acid; Spectrophotometry, Ultraviolet; Stereoisomerism | 1996 |
Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding.
Topics: Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin Mononucleotide; Kinetics; Models, Molecular; Oxidation-Reduction; Phosphorus-Oxygen Lyases; Protein Conformation; Protein Denaturation; Scattering, Radiation; Shikimic Acid; Solubility; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Trypsin; Tryptophan; Ultraviolet Rays | 1998 |
Studies with substrate and cofactor analogues provide evidence for a radical mechanism in the chorismate synthase reaction.
Topics: Benzoquinones; Chromatography, High Pressure Liquid; Dithionite; Escherichia coli; Flavin Mononucleotide; Inhibitory Concentration 50; Kinetics; Magnetic Resonance Spectroscopy; Molecular Structure; Organophosphorus Compounds; Oxidation-Reduction; Phosphorus-Oxygen Lyases; Recombinant Proteins; Shikimic Acid; Spectrophotometry | 2000 |
Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa: evidence for a common binding site for 5-enolpyruvylshikimate 3-phosphate and NADPH.
Topics: Binding Sites; Cloning, Molecular; DNA, Complementary; Escherichia coli; Flavin Mononucleotide; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; NADP; Neurospora crassa; Oxidoreductases; Oxygen; Phosphorus-Oxygen Lyases; Plasmids; Protein Binding; Protein Structure, Tertiary; Shikimic Acid; Spectrometry, Fluorescence; Spectrophotometry; Substrate Specificity; Time Factors; Ultraviolet Rays | 2001 |
Replacement of two invariant serine residues in chorismate synthase provides evidence that a proton relay system is essential for intermediate formation and catalytic activity.
Topics: Alanine; Amino Acid Substitution; Catalysis; Flavin Mononucleotide; Flavins; Histidine; Hydrogen Bonding; Mutagenesis, Site-Directed; Neurospora crassa; Phosphorus-Oxygen Lyases; Protein Binding; Protons; Serine; Shikimic Acid; Substrate Specificity | 2008 |