Compounds > methylacetylphosphonate
Page last updated: 2024-09-05

methylacetylphosphonate and thiamine pyrophosphate

methylacetylphosphonate has been researched along with thiamine pyrophosphate in 3 studies

Compound Research Comparison

Studies
(methylacetylphosphonate)		Trials
(methylacetylphosphonate)		Recent Studies (post-2010)
(methylacetylphosphonate)		Studies
(thiamine pyrophosphate)		Trials
(thiamine pyrophosphate)		Recent Studies (post-2010) (thiamine pyrophosphate)
19032,44429320

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's0 (0.00)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Gennis, RB; Kluger, R; O'Brien, TA; Pike, DC1
Baykal, A; Furey, W; Jordan, F; Joseph, E; Nemeria, N; Yan, Y; Zhang, S1
Arens, J; Golbik, R; Meyer, D; Schröder-Tittmann, K; Tietzel, M; Tittmann, K; Wechsler, C1

Other Studies

3 other study(ies) available for methylacetylphosphonate and thiamine pyrophosphate

ArticleYear
Phosphonate analogues of pyruvate. Probes of substrate binding to pyruvate oxidase and other thiamin pyrophosphate-dependent decarboxylases.
    Biochimica et biophysica acta, 1980, Volume: 613, Issue:1

    Topics: Acetaldehyde; Circular Dichroism; Enzyme Activation; Escherichia coli; Kinetics; Lipids; Organophosphorus Compounds; Phosphonoacetic Acid; Pyruvate Decarboxylase; Pyruvate Dehydrogenase Complex; Pyruvate Oxidase; Pyruvates; Thiamine Pyrophosphate

1980
Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1',4'-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme.
    Biochemistry, 2004, Jun-01, Volume: 43, Issue:21

    Topics: Binding Sites; Catalysis; Circular Dichroism; Coenzymes; Decarboxylation; Fungal Proteins; Models, Chemical; Models, Molecular; Phosphonoacetic Acid; Point Mutation; Protein Conformation; Pyruvate Decarboxylase; Pyruvate Dehydrogenase Complex; Thiamine Pyrophosphate; Titrimetry

2004
Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding.
    Biochemistry, 2013, Apr-16, Volume: 52, Issue:15

    Topics: Acetolactate Synthase; Binding Sites; Calorimetry; Catalytic Domain; Enzymes; Escherichia coli Proteins; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Phosphonoacetic Acid; Protein Binding; Pyruvate Dehydrogenase (Lipoamide); Pyruvate Oxidase; Thermodynamics; Thiamine Pyrophosphate

2013