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fructose-6-phosphate and tryptophan

fructose-6-phosphate has been researched along with tryptophan in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (66.67)18.2507
2000's2 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Auzat, I; Garel, JR; Gawlita, E1
Johnson, JL; Reinhart, GD1
Babul, J; Guixé, V; Rodríguez, PH1
Hasemann, CA; Hazlett, TL; Helms, MK; Jameson, DM; Mizuguchi, H; Uyeda, K1
Reinhart, GD; Riley-Lovingshimer, MR; Ronning, DR; Sacchettini, JC1
Reinhart, GD; Riley-Lovingshimer, MR1

Other Studies

6 other study(ies) available for fructose-6-phosphate and tryptophan

ArticleYear
Slow ligand-induced transitions in the allosteric phosphofructokinase from Escherichia coli.
    Journal of molecular biology, 1995, Jun-02, Volume: 249, Issue:2

    Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Allosteric Regulation; Allosteric Site; Crystallography, X-Ray; Escherichia coli; Fructosephosphates; Kinetics; Ligands; Phosphoenolpyruvate; Phosphofructokinase-1; Protein Conformation; Spectrometry, Fluorescence; Time Factors; Tryptophan

1995
Influence of MgADP on phosphofructokinase from Escherichia coli. Elucidation of coupling interactions with both substrates.
    Biochemistry, 1994, Mar-08, Volume: 33, Issue:9

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Allosteric Regulation; Binding Sites; Escherichia coli; Fructosephosphates; Kinetics; Ligands; Phosphofructokinase-1; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

1994
Ligand-induced conformational transitions in Escherichia coli phosphofructokinase 2: evidence for an allosteric site for MgATP2-.
    Biochemistry, 1998, Sep-22, Volume: 37, Issue:38

    Topics: Adenosine Triphosphate; Allosteric Site; Escherichia coli; Fluorescence Polarization; Fructosephosphates; Kinetics; Ligands; Phosphofructokinase-1; Protein Conformation; Spectrometry, Fluorescence; Tryptophan

1998
Site-directed mutants of rat testis fructose 6-phosphate, 2-kinase/fructose 2,6-bisphosphatase: localization of conformational alterations induced by ligand binding.
    Biochemistry, 1998, Oct-06, Volume: 37, Issue:40

    Topics: Amino Acid Substitution; Animals; Fluorescence Polarization; Fructosediphosphates; Fructosephosphates; Ligands; Male; Multienzyme Complexes; Mutagenesis, Site-Directed; Phenylalanine; Phosphofructokinase-2; Phosphoric Monoester Hydrolases; Phosphotransferases; Protein Binding; Protein Conformation; Rats; Testis; Tryptophan

1998
Reversible ligand-induced dissociation of a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus.
    Biochemistry, 2002, Oct-29, Volume: 41, Issue:43

    Topics: Allosteric Site; Crystallography, X-Ray; Dimerization; Enzyme Inhibitors; Enzyme Reactivators; Fructosephosphates; Geobacillus stearothermophilus; Ligands; Mutagenesis, Site-Directed; Phosphoenolpyruvate; Phosphofructokinase-1; Spectrometry, Fluorescence; Tryptophan; Tyrosine

2002
Examination of MgATP binding in a tryptophan-shift mutant of phosphofructokinase from Bacillus stearothermophilus.
    Archives of biochemistry and biophysics, 2005, Apr-01, Volume: 436, Issue:1

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Allosteric Site; Base Sequence; Binding Sites; Fructosephosphates; Genetic Variation; Geobacillus stearothermophilus; Mutation; Phosphoenolpyruvate; Phosphofructokinases; Spectrometry, Fluorescence; Tryptophan

2005