thiamine pyrophosphate and glutamic acid

thiamine pyrophosphate has been researched along with glutamic acid in 17 studies

Research

Studies (17)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's5 (29.41)18.2507
2000's5 (29.41)29.6817
2010's6 (35.29)24.3611
2020's1 (5.88)2.80

Authors

AuthorsStudies
Lindqvist, Y; Meshalkina, L; Nikkola, M; Nilsson, U; Schneider, G; Sundström, M; Wikner, C1
Candy, JM; Duggleby, RG; Koga, J; Nixon, PF1
Hübner, G; Kern, D; Kern, G; Killenberg-Jabs, M; Neef, H; Schneider, G; Tittmann, K; Wikner, C1
Duggleby, RG; Fang, R; Nixon, PF1
Chang, AK; Duggleby, RG; Nixon, PF1
Furey, W; Guo, F; Hübner, G; Jordan, F; Liu, M; Sergienko, EA; Tittmann, K; Wang, J1
Jordan, F1
Arjunan, P; Furey, W; Hübner, G; Jordan, F; Joseph, E; Nemeria, N; Tittmann, K; Vazquez-Coll, MB; Zhou, L1
Batifoulier, F; Besson, C; Chanliaud, E; Demigné, C; Rémésy, C; Verny, MA1
Chipman, DM; Shaanan, B1
Friedemann, R; Jordan, F; Meyer, D; Nemeria, N; Neumann, P; Parthier, C; Tittmann, K1
Balakrishnan, A; Barak, Z; Binshtein, E; Chipman, D; Jordan, F; Nemeria, N; Patel, H; Shaanan, B; Vered, I1
Baig, IA; Kim, MS; Koo, BS; Moon, JY; Yoon, MY1
Arena de Souza, V; Bumann, M; Lobley, CM; Lukacik, P; O'Toole, PW; Owens, RJ; Walsh, MA1
Bettendorff, L; Bunik, V; Graf, A; Mkrtchyan, G1
Mata, RA; Paulikat, M; Tittmann, K; Wechsler, C1
Aldeghi, M; Begley, T; de Groot, BL; Rabe von Pappenheim, F; Shome, B; Tittmann, K1

Reviews

1 review(s) available for thiamine pyrophosphate and glutamic acid

ArticleYear
Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue.
    The FEBS journal, 2009, Volume: 276, Issue:9

    Topics: Crystallography, X-Ray; Glutamic Acid; Kinetics; Protein Conformation; Substrate Specificity; Thiamine Pyrophosphate

2009

Other Studies

16 other study(ies) available for thiamine pyrophosphate and glutamic acid

ArticleYear
Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis.
    The Journal of biological chemistry, 1994, Dec-23, Volume: 269, Issue:51

    Topics: Animals; Catalysis; Cell Line; Circular Dichroism; Crystallography, X-Ray; Glutamic Acid; Mutagenesis, Site-Directed; Rabbits; Recombinant Proteins; Thiamine Pyrophosphate; Transketolase

1994
The role of residues glutamate-50 and phenylalanine-496 in Zymomonas mobilis pyruvate decarboxylase.
    The Biochemical journal, 1996, May-01, Volume: 315 ( Pt 3)

    Topics: Amino Acid Sequence; Binding Sites; Escherichia coli; Glutamic Acid; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Phenylalanine; Protein Conformation; Pyruvate Decarboxylase; Recombinant Proteins; Sequence Homology, Amino Acid; Thiamine Pyrophosphate; Zymomonas

1996
How thiamine diphosphate is activated in enzymes.
    Science (New York, N.Y.), 1997, Jan-03, Volume: 275, Issue:5296

    Topics: Allosteric Regulation; Binding Sites; Catalysis; Deuterium; Enzyme Activation; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Protons; Pyruvate Decarboxylase; Pyruvates; Thermodynamics; Thiamine Pyrophosphate; Transketolase

1997
Identification of the catalytic glutamate in the E1 component of human pyruvate dehydrogenase.
    FEBS letters, 1998, Oct-23, Volume: 437, Issue:3

    Topics: Amino Acid Sequence; Catalytic Domain; Glutamic Acid; Humans; Kinetics; Molecular Sequence Data; Protein Binding; Pyruvate Dehydrogenase (Lipoamide); Pyruvate Dehydrogenase Complex; Recombinant Proteins; Sequence Alignment; Thiamine Pyrophosphate

1998
Aspartate-27 and glutamate-473 are involved in catalysis by Zymomonas mobilis pyruvate decarboxylase.
    The Biochemical journal, 1999, Apr-15, Volume: 339 ( Pt 2)

    Topics: Aspartic Acid; Catalysis; Electrophoresis, Polyacrylamide Gel; Glutamic Acid; Kinetics; Mutagenesis, Site-Directed; Protein Conformation; Pyruvate Decarboxylase; Substrate Specificity; Thiamine Pyrophosphate; Zymomonas

1999
Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions.
    Biochemistry, 2001, Jun-26, Volume: 40, Issue:25

    Topics: Alanine; Amino Acid Substitution; Aspartic Acid; Carbon Dioxide; Catalysis; Catalytic Domain; Cloning, Molecular; DNA, Recombinant; Enzyme Activation; Glutamic Acid; Glutamine; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Pyruvate Decarboxylase; Recombinant Proteins; Saccharomyces cerevisiae; Substrate Specificity; Thiamine Pyrophosphate

2001
Biochemistry. How active sites communicate in thiamine enzymes.
    Science (New York, N.Y.), 2004, Oct-29, Volume: 306, Issue:5697

    Topics: Amino Acid Substitution; Binding Sites; Dihydrolipoyllysine-Residue Acetyltransferase; Dimerization; Geobacillus stearothermophilus; Glutamic Acid; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Protons; Pyruvate Dehydrogenase (Lipoamide); Pyruvate Dehydrogenase Complex; Thiamine Pyrophosphate

2004
Glutamate 636 of the Escherichia coli pyruvate dehydrogenase-E1 participates in active center communication and behaves as an engineered acetolactate synthase with unusual stereoselectivity.
    The Journal of biological chemistry, 2005, Jun-03, Volume: 280, Issue:22

    Topics: Acetolactate Synthase; Aspartic Acid; Binding Sites; Catalysis; Circular Dichroism; Dose-Response Relationship, Drug; Escherichia coli; Genetic Variation; Glutamic Acid; Kinetics; Lactates; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Oxygen; Peptides; Plasmids; Protein Binding; Protein Structure, Tertiary; Pyrimidine Nucleosides; Pyruvate Dehydrogenase (Lipoamide); Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectroscopy, Fourier Transform Infrared; Stereoisomerism; Temperature; Thiamine Pyrophosphate; Trypsin; Ultraviolet Rays

2005
Restoration of thiamine status with white or whole wheat bread in a thiamine-depleted rat model.
    International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition, 2007, Volume: 77, Issue:1

    Topics: Animals; Body Weight; Bread; Cerebellum; Diet; Disease Models, Animal; Glucose; Glutamic Acid; Kidney; Lactic Acid; Liver; Pyruvic Acid; Rats; Rats, Wistar; Thiamine; Thiamine Deficiency; Thiamine Pyrophosphate; Triticum

2007
Double duty for a conserved glutamate in pyruvate decarboxylase: evidence of the participation in stereoelectronically controlled decarboxylation and in protonation of the nascent carbanion/enamine intermediate .
    Biochemistry, 2010, Sep-21, Volume: 49, Issue:37

    Topics: Amines; Binding Sites; Catalysis; Crystallography, X-Ray; Decarboxylation; Glutamic Acid; Thermodynamics; Thiamine Pyrophosphate; X-Rays; Zymomonas

2010
Glyoxylate carboligase: a unique thiamin diphosphate-dependent enzyme that can cycle between the 4'-aminopyrimidinium and 1',4'-iminopyrimidine tautomeric forms in the absence of the conserved glutamate.
    Biochemistry, 2012, Oct-09, Volume: 51, Issue:40

    Topics: Amino Acid Substitution; Circular Dichroism; Gene Expression Regulation; Glutamic Acid; Hydrogen-Ion Concentration; Ligases; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Pyrimidines; Pyruvic Acid; Substrate Specificity; Thiamine Pyrophosphate

2012
Structural and functional significance of the highly-conserved residues in Mycobacterium tuberculosis acetohydroxyacid synthase.
    Enzyme and microbial technology, 2014, May-10, Volume: 58-59

    Topics: Acetolactate Synthase; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalysis; Conserved Sequence; Dimerization; Escherichia coli; Glutamic Acid; Models, Molecular; Molecular Dynamics Simulation; Molecular Sequence Data; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; Protein Conformation; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship; Thiamine Pyrophosphate

2014
High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophosphate.
    Acta crystallographica. Section F, Structural biology communications, 2015, Volume: 71, Issue:Pt 10

    Topics: Apoproteins; Catalytic Domain; Coenzymes; Crystallization; Crystallography, X-Ray; Glutamic Acid; Lactobacillus; Models, Molecular; Phylogeny; Protein Structure, Secondary; Solutions; Structural Homology, Protein; Thiamine Pyrophosphate; Transketolase

2015
Cellular thiamine status is coupled to function of mitochondrial 2-oxoglutarate dehydrogenase.
    Neurochemistry international, 2016, Volume: 101

    Topics: Animals; Cerebral Cortex; Cytoplasm; Glutamic Acid; Homeostasis; Ketoglutarate Dehydrogenase Complex; Mice; Mitochondria; Organophosphonates; Succinates; Thiamine; Thiamine Pyrophosphate

2016
Theoretical Studies of the Electronic Absorption Spectra of Thiamin Diphosphate in Pyruvate Decarboxylase.
    Biochemistry, 2017, 04-04, Volume: 56, Issue:13

    Topics: Bacterial Proteins; Catalytic Domain; Coenzymes; Electron Transport; Gene Expression; Glutamic Acid; Kinetics; Molecular Dynamics Simulation; Mutation; Protein Structure, Secondary; Pyrimidines; Pyruvate Decarboxylase; Static Electricity; Thermodynamics; Thiamine Pyrophosphate; Zymomonas

2017
Structural basis for antibiotic action of the B
    Nature chemical biology, 2020, Volume: 16, Issue:11

    Topics: Amino Acid Sequence; Anti-Bacterial Agents; Catalytic Domain; Coenzymes; Drug Design; Enzyme Inhibitors; Escherichia coli; Glutamic Acid; Humans; Hydrogen Bonding; Kinetics; Molecular Dynamics Simulation; Molecular Structure; Protein Binding; Structure-Activity Relationship; Substrate Specificity; Thiamine; Thiamine Pyrophosphate; Transketolase

2020