indoleglycerol phosphate and serine

indoleglycerol phosphate has been researched along with serine in 11 studies

Research

Studies (11)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's7 (63.64)18.2507
2000's2 (18.18)29.6817
2010's2 (18.18)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Miles, EW; Yang, XJ1
Brzović, PS; Dunn, MF; Ngo, K1
Kirschner, K; Lane, AN; Strasser, AW1
Anderson, KS; Johnson, KA; Miles, EW1
Dunn, MF; Woehl, EU1
Anderson, KS; Kim, AY; Miles, EW; Schlichting, I; Yang, XJ1
Anderson, KS; Kim, AY; Miles, EW; Quillen, JM; Sayers, E; Yang, XJ1
Barends, TR; Blumenstein, L; Casino, P; Dunn, MF; Harris, R; Kimmich, N; Kulik, V; Ngo, H; Niks, D; Schlichting, I; Weyand, M1
Dierkers, AT; Dunn, MF; Niks, D; Schlichting, I1
Arnold, FH; Buller, AR; Murciano-Calles, J; van Roye, P1
Eisbach, M; Loutchko, D; Mikhailov, AS1

Other Studies

11 other study(ies) available for indoleglycerol phosphate and serine

ArticleYear
Threonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex.
    The Journal of biological chemistry, 1992, Apr-15, Volume: 267, Issue:11

    Topics: Amino Acid Sequence; Catalysis; Electrophoresis, Polyacrylamide Gel; Fluorescence; Glycerophosphates; Hydrolysis; Indoles; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Salmonella typhimurium; Serine; Threonine; Tryptophan Synthase

1992
Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex.
    Biochemistry, 1992, Apr-21, Volume: 31, Issue:15

    Topics: Alanine; Allosteric Regulation; Catalysis; Glycerophosphates; Indoles; Kinetics; Multienzyme Complexes; Protein Conformation; Salmonella typhimurium; Serine; Spectrum Analysis; Tryptophan Synthase

1992
Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex.
    Biochemistry, 1991, Jan-15, Volume: 30, Issue:2

    Topics: Binding Sites; Escherichia coli; Glycerophosphates; Hydrogen-Ion Concentration; Indoles; Kinetics; Ligands; Multienzyme Complexes; Osmolar Concentration; Protein Conformation; Serine; Spectrum Analysis; Tryptophan Synthase

1991
Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism.
    The Journal of biological chemistry, 1991, May-05, Volume: 266, Issue:13

    Topics: Binding Sites; Chromatography, High Pressure Liquid; Computer Simulation; Fluorescence; Glycerophosphates; Indoles; Kinetics; Molecular Structure; Mutation; Protein Conformation; Salmonella typhimurium; Serine; Substrate Specificity; Tryptophan; Tryptophan Synthase

1991
Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex.
    Biochemistry, 1995, Jul-25, Volume: 34, Issue:29

    Topics: Binding Sites; Catalysis; Cations, Monovalent; Glycerophosphates; Kinetics; Macromolecular Substances; Mathematics; Models, Theoretical; Potassium; Salmonella typhimurium; Serine; Sodium; Spectrophotometry; Time Factors; Tryptophan; Tryptophan Synthase

1995
Structural and kinetic analysis of a channel-impaired mutant of tryptophan synthase.
    The Journal of biological chemistry, 1994, Oct-28, Volume: 269, Issue:43

    Topics: Catalysis; Crystallography, X-Ray; Glycerophosphates; Indoles; Kinetics; Models, Molecular; Mutation; Salmonella typhimurium; Serine; Tryptophan; Tryptophan Synthase

1994
Kinetic characterization of channel impaired mutants of tryptophan synthase.
    The Journal of biological chemistry, 1995, Dec-15, Volume: 270, Issue:50

    Topics: Binding Sites; Carbon Radioisotopes; Glycerophosphates; Indoles; Kinetics; Macromolecular Substances; Mathematics; Models, Theoretical; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Radioisotope Dilution Technique; Recombinant Proteins; Salmonella typhimurium; Serine; Structure-Activity Relationship; Tryptophan Synthase

1995
Synthesis and characterization of allosteric probes of substrate channeling in the tryptophan synthase bienzyme complex.
    Biochemistry, 2007, Jul-03, Volume: 46, Issue:26

    Topics: Allosteric Regulation; Anilino Naphthalenesulfonates; Binding Sites; Glyceraldehyde 3-Phosphate; Glycerophosphates; Kinetics; Models, Chemical; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Salmonella typhimurium; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan Synthase

2007
Tryptophan synthase: structure and function of the monovalent cation site.
    Biochemistry, 2009, Nov-24, Volume: 48, Issue:46

    Topics: Binding Sites; Biocatalysis; Cations, Monovalent; Cesium; Computer Simulation; Glycerophosphates; Histidine; Indoles; Kinetics; Models, Chemical; Models, Molecular; Protein Conformation; Pyruvic Acid; Quaternary Ammonium Compounds; Salmonella typhimurium; Serine; Sodium; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan Synthase

2009
Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity.
    Biochemistry, 2016, Dec-27, Volume: 55, Issue:51

    Topics: Allosteric Regulation; Archaeal Proteins; Binding Sites; Biocatalysis; Biosynthetic Pathways; Crystallography, X-Ray; Glycerophosphates; Indoles; Kinetics; Models, Molecular; Molecular Structure; Protein Binding; Protein Domains; Protein Subunits; Pyrococcus furiosus; Serine; Spectrophotometry; Substrate Specificity; Threonine; Tryptophan; Tryptophan Synthase

2016
Stochastic thermodynamics of a chemical nanomachine: The channeling enzyme tryptophan synthase.
    The Journal of chemical physics, 2017, Jan-14, Volume: 146, Issue:2

    Topics: Allosteric Regulation; Entropy; Glycerophosphates; Models, Biological; Molecular Structure; Nanostructures; Protein Subunits; Serine; Stochastic Processes; Thermodynamics; Tryptophan; Tryptophan Synthase

2017