Compounds > thiamine pyrophosphate

thiamine pyrophosphate and phenylalanine

thiamine pyrophosphate has been researched along with phenylalanine in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's2 (40.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Arnon, DI; Gehring, U1
Candy, JM; Duggleby, RG; Koga, J; Nixon, PF1
Jordan, F; Li, H1
Furey, W; Guo, F; Hübner, G; Jordan, F; Liu, M; Sergienko, EA; Tittmann, K; Wang, J1
Morais, MA; Piper, MD; Pronk, JT; Tai, SL; Vuralhan, Z1

Other Studies

5 other study(ies) available for thiamine pyrophosphate and phenylalanine

ArticleYear
Ferredoxin-dependent phenylpyruvate synthesis by cell-free preparations of photosynthetic bacteria.
    The Journal of biological chemistry, 1971, Jul-25, Volume: 246, Issue:14

    Topics: Adenosine Triphosphate; Autoradiography; Bacteria; Bicarbonates; Carbon Isotopes; Cell Fractionation; Cell-Free System; Chlorides; Chloroplasts; Chromatium; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Paper; Chromatography, Thin Layer; Clostridium; Coenzyme A; Ferredoxins; Glutamates; Hydrogen-Ion Concentration; Magnesium; Oxidation-Reduction; Phenylacetates; Phenylalanine; Phenylpyruvic Acids; Plants; Thiamine Pyrophosphate; Ultracentrifugation

1971
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
Effects of substitution of tryptophan 412 in the substrate activation pathway of yeast pyruvate decarboxylase.
    Biochemistry, 1999, Aug-03, Volume: 38, Issue:31

    Topics: Alanine; Amino Acid Substitution; Apoenzymes; Binding Sites; Circular Dichroism; Enzyme Activation; Enzyme Stability; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Protein Structure, Tertiary; Pyruvate Decarboxylase; Recombinant Proteins; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Substrate Specificity; Thiamine Pyrophosphate; Tryptophan

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
Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae.
    Applied and environmental microbiology, 2003, Volume: 69, Issue:8

    Topics: Carboxy-Lyases; Phenylalanine; Phenylpyruvic Acids; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity; Thiamine Pyrophosphate; Transcription, Genetic

2003