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2-hydroxy-3-butynoate and lactic acid

2-hydroxy-3-butynoate has been researched along with lactic acid in 2 studies

*Lactic Acid: A normal intermediate in the fermentation (oxidation, metabolism) of sugar. The concentrated form is used internally to prevent gastrointestinal fermentation. (From Stedman, 26th ed) [MeSH]

*Lactic Acid: A normal intermediate in the fermentation (oxidation, metabolism) of sugar. The concentrated form is used internally to prevent gastrointestinal fermentation. (From Stedman, 26th ed) [MeSH]

Compound Research Comparison

Studies
(2-hydroxy-3-butynoate)
Trials
(2-hydroxy-3-butynoate)
Recent Studies (post-2010)
(2-hydroxy-3-butynoate)
Studies
(lactic acid)
Trials
(lactic acid)
Recent Studies (post-2010) (lactic acid)
110246,2633,34919,053

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (50.00)18.2507
2000's0 (0.00)29.6817
2010's1 (50.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chapman, SK; Dubois, J; Lederer, F; Mathews, FS; Reid, GA1
Bodevin, S; Lederer, F; North, P; Vignaud, C1

Other Studies

2 other study(ies) available for 2-hydroxy-3-butynoate and lactic acid

ArticleYear
Substitution of Tyr254 with Phe at the active site of flavocytochrome b2: consequences on catalysis of lactate dehydrogenation.
    Biochemistry, 1990, Jul-10, Volume: 29, Issue:27

    Topics: Binding Sites; Catalysis; Deuterium; Fungal Proteins; Hydroxybutyrates; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactates; Lactic Acid; Models, Molecular; Phenylalanine; Protein Conformation; Pyruvates; Saccharomyces cerevisiae; Tyrosine

1990
Trifluorosubstrates as mechanistic probes for an FMN-dependent l-2-hydroxy acid-oxidizing enzyme.
    Biochimica et biophysica acta, 2016, Volume: 1864, Issue:9

    Topics: Binding Sites; Biocatalysis; Catalytic Domain; Flavin Mononucleotide; Halogenation; Humans; Hydrogen Bonding; Hydroxybutyrates; Kinetics; L-Lactate Dehydrogenase; L-Lactate Dehydrogenase (Cytochrome); Lactic Acid; Protein Binding; Protein Domains; Protons; Pyruvic Acid; Recombinant Proteins; Substrate Specificity

2016