Page last updated: 2024-08-21

chorismic acid and tryptophan

chorismic acid has been researched along with tryptophan in 16 studies

Research

Studies (16)

TimeframeStudies, this research(%)All Research%
pre-19904 (25.00)18.7374
1990's2 (12.50)18.2507
2000's6 (37.50)29.6817
2010's4 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Pittard, J; Tribe, DE1
Levy, HR; Nowak, T; Robison, PD1
Crawford, IP1
Katz, E; Murphy, MF1
Braus, G; Lipscomb, WN; Schnappauf, G; Sträter, N1
Braus, GH; Eckert, S; Gerstberger, T; Helmstaedt, K; Hoffmann, B; Hoppert, M; Krappmann, S; Schnappauf, G1
Byrnes, WM; Goldberg, RN; Holden, MJ; Mayhew, MP; Tewari, YB1
Atomi, H; Ezaki, S; Imanaka, T; Tang, XF1
Kim, C; Mills, SE; Nguyen-Huu, X; Spraggon, G; Yanofsky, C; Yee, MC1
Bonner, CA; Gosset, G; Jensen, RA1
Eisenstein, E; Howard, AJ; Jensen, PY; Ladner, JE; Pachikara, AS; Parsons, JF1
Farrow, JM; Pesci, EC1
Ma, L; Payne, SM1
Coleman, JP; Knoten, CA; Pesci, EC; Wells, G1
Jez, JM; Westfall, CS; Xu, A1
Gulick, AM; Lamb, AL; Meneely, KM; Moran, GR; Sundlov, JA1

Other Studies

16 other study(ies) available for chorismic acid and tryptophan

ArticleYear
Hyperproduction of tryptophan by Escherichia coli: genetic manipulation of the pathways leading to tryptophan formation.
    Applied and environmental microbiology, 1979, Volume: 38, Issue:2

    Topics: 3-Deoxy-7-Phosphoheptulonate Synthase; Anthranilate Synthase; Chorismic Acid; Escherichia coli; Genetic Engineering; Glucose; Isoenzymes; Mutation; Quaternary Ammonium Compounds; Transduction, Genetic; Tryptophan; Tryptophan Synthase

1979
Magnetic resonance studies of the anthranilate synthetase-phosphoribosyltransferase enzyme complex from Salmonella typhimurium.
    Archives of biochemistry and biophysics, 1979, Volume: 193, Issue:1

    Topics: Anthranilate Phosphoribosyltransferase; Anthranilate Synthase; Binding Sites; Chorismic Acid; Electron Spin Resonance Spectroscopy; Manganese; Pentosyltransferases; Protein Binding; Salmonella typhimurium; Tryptophan

1979
Synthesis of tryptophan from chorismate: comparative aspects.
    Methods in enzymology, 1987, Volume: 142

    Topics: Chorismic Acid; Cyclohexanecarboxylic Acids; Enterobacteriaceae; Escherichia coli; Fungi; Genes, Bacterial; Gram-Negative Bacteria; Gram-Positive Bacteria; Operon; Tryptophan

1987
Regulatory control of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase in Streptomyces antibioticus.
    Canadian journal of microbiology, 1980, Volume: 26, Issue:8

    Topics: 3-Deoxy-7-Phosphoheptulonate Synthase; Aldehyde-Lyases; Chorismic Acid; Enzyme Repression; Hydrogen-Ion Concentration; Kinetics; Phenylalanine; Streptomyces; Streptomyces antibioticus; Tryptophan; Tyrosine

1980
Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
    Structure (London, England : 1993), 1997, Nov-15, Volume: 5, Issue:11

    Topics: Bacillus subtilis; Binding Sites; Bridged Bicyclo Compounds; Chorismate Mutase; Chorismic Acid; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Models, Molecular; Mutation; Protein Conformation; Tryptophan; Tyrosine; Yeasts

1997
The aroC gene of Aspergillus nidulans codes for a monofunctional, allosterically regulated chorismate mutase.
    The Journal of biological chemistry, 1999, Aug-06, Volume: 274, Issue:32

    Topics: Allosteric Regulation; Amino Acid Sequence; Aspartic Acid; Aspergillus nidulans; Chorismate Mutase; Chorismic Acid; Computer Simulation; Genes, Fungal; Hydrogen-Ion Concentration; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphorus-Oxygen Lyases; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid; Tryptophan; Tyrosine

1999
Thermodynamics of reactions catalyzed by anthranilate synthase.
    Biophysical chemistry, 2000, Feb-14, Volume: 84, Issue:1

    Topics: Anthranilate Synthase; Calorimetry; Catalysis; Cations; Chorismic Acid; Escherichia coli; Hydrogen-Ion Concentration; Kinetics; Recombinant Proteins; Thermodynamics; Tryptophan

2000
Anthranilate synthase without an LLES motif from a hyperthermophilic archaeon is inhibited by tryptophan.
    Biochemical and biophysical research communications, 2001, Mar-09, Volume: 281, Issue:4

    Topics: Amino Acid Motifs; Amino Acid Sequence; Ammonium Chloride; Anthranilate Synthase; Chorismic Acid; Escherichia coli; Gene Expression Regulation, Enzymologic; Genes, Archaeal; Glutamine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Amino Acid; Temperature; Thermococcus; Tryptophan

2001
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
    Proceedings of the National Academy of Sciences of the United States of America, 2001, May-22, Volume: 98, Issue:11

    Topics: Amino Acid Sequence; Anthranilate Synthase; Base Sequence; Binding Sites; Chorismic Acid; Crystallography, X-Ray; Cyclohexenes; DNA, Bacterial; Glutamic Acid; Glutamine; Lyases; Molecular Sequence Data; Nitrogenous Group Transferases; Oligopeptides; ortho-Aminobenzoates; Protein Structure, Secondary; Serratia marcescens; Substrate Specificity; Tryptophan

2001
Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris.
    Journal of bacteriology, 2001, Volume: 183, Issue:13

    Topics: 3-Deoxy-7-Phosphoheptulonate Synthase; Allosteric Regulation; Amino Acid Motifs; Amino Acid Sequence; Base Sequence; Cations, Divalent; Chorismic Acid; Cloning, Molecular; Dithiothreitol; Enzyme Stability; Evolution, Molecular; Feedback; Genetic Complementation Test; Kinetics; Molecular Sequence Data; Phylogeny; Plant Proteins; Plants; Recombinant Proteins; Temperature; Tryptophan; Xanthomonas campestris

2001
Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes.
    Biochemistry, 2002, Feb-19, Volume: 41, Issue:7

    Topics: Amino Acid Sequence; Binding Sites; Carbon-Nitrogen Ligases; Chorismic Acid; Conserved Sequence; Crystallization; Crystallography, X-Ray; Escherichia coli; Evolution, Molecular; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship; Transaminases; Tryptophan

2002
Two distinct pathways supply anthranilate as a precursor of the Pseudomonas quinolone signal.
    Journal of bacteriology, 2007, Volume: 189, Issue:9

    Topics: Antibiosis; Artificial Gene Fusion; beta-Galactosidase; Chorismic Acid; Gene Deletion; Gene Expression Regulation, Bacterial; Genetic Complementation Test; Kynurenine; Metabolic Networks and Pathways; Microbial Viability; Models, Biological; ortho-Aminobenzoates; Pseudomonas aeruginosa; Quinolones; Staphylococcus aureus; Tryptophan

2007
AhpC is required for optimal production of enterobactin by Escherichia coli.
    Journal of bacteriology, 2012, Volume: 194, Issue:24

    Topics: Chorismic Acid; Culture Media; Enterobactin; Escherichia coli; Escherichia coli Proteins; Gene Deletion; Hydroxybenzoates; Iron; para-Aminobenzoates; Peroxiredoxins; Phenylalanine; Shikimic Acid; Tryptophan; Tyrosine

2012
A conserved suppressor mutation in a tryptophan auxotroph results in dysregulation of Pseudomonas quinolone signal synthesis.
    Journal of bacteriology, 2014, Volume: 196, Issue:13

    Topics: Chorismic Acid; Gene Expression Regulation, Bacterial; Molecular Structure; Mutation; ortho-Aminobenzoates; Polymerase Chain Reaction; Pseudomonas aeruginosa; Quinolones; Tryptophan

2014
Structural evolution of differential amino acid effector regulation in plant chorismate mutases.
    The Journal of biological chemistry, 2014, Oct-10, Volume: 289, Issue:41

    Topics: Allosteric Regulation; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Chorismate Mutase; Chorismic Acid; Crystallography, X-Ray; Enzyme Activation; Escherichia coli; Evolution, Molecular; Gene Expression; Isoenzymes; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Phenylalanine; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Tryptophan; Tyrosine

2014
An Open and Shut Case: The Interaction of Magnesium with MST Enzymes.
    Journal of the American Chemical Society, 2016, 07-27, Volume: 138, Issue:29

    Topics: Binding Sites; Catalytic Domain; Chorismic Acid; Intramolecular Transferases; Kinetics; Magnesium; Models, Molecular; Protein Binding; Siderophores; Tryptophan; Vitamin K 2

2016