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3-acetylpyridine adenine dinucleotide and deuterium

3-acetylpyridine adenine dinucleotide has been researched along with deuterium in 5 studies

Compound Research Comparison

Studies
(3-acetylpyridine adenine dinucleotide)
Trials
(3-acetylpyridine adenine dinucleotide)
Recent Studies (post-2010)
(3-acetylpyridine adenine dinucleotide)
Studies
(deuterium)
Trials
(deuterium)
Recent Studies (post-2010) (deuterium)
680213,1042172,527

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's3 (60.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cleland, WW; Cook, PF; Gavva, SR; Harris, BG; Urbauer, JL; Weiss, PM1
Morrison, JF; Stone, SR1
Cleland, WW; Hermes, JD; Morrical, SW; O'Leary, MH1
Claiborne, A; Crane, EJ; Parsonage, D; Poole, LB1
Bradshaw, DE; Cleland, WW; Urbauer, JL1

Other Studies

5 other study(ies) available for 3-acetylpyridine adenine dinucleotide and deuterium

ArticleYear
Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
    Biochemistry, 1991, Jun-11, Volume: 30, Issue:23

    Topics: Animals; Ascaris; Carbon Isotopes; Chickens; Decarboxylation; Deuterium; Kinetics; Liver; Malate Dehydrogenase; Malates; NAD; NADP; Oxidation-Reduction; Substrate Specificity

1991
Dihydrofolate reductase from Escherichia coli: the kinetic mechanism with NADPH and reduced acetylpyridine adenine dinucleotide phosphate as substrates.
    Biochemistry, 1988, Jul-26, Volume: 27, Issue:15

    Topics: Deuterium; Escherichia coli; Folic Acid; Hydrogen-Ion Concentration; Kinetics; NAD; NADP; Tetrahydrofolate Dehydrogenase; Viscosity

1988
Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase.
    Biochemistry, 1984, Nov-06, Volume: 23, Issue:23

    Topics: Aldehyde Oxidoreductases; Carbon Isotopes; Chemical Phenomena; Chemistry; Deuterium; Formate Dehydrogenases; Formates; Kinetics; NAD; Nitrogen Isotopes; Oxidation-Reduction; Oxygen Isotopes; Saccharomyces cerevisiae

1984
Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron-reduced enzyme forms.
    Biochemistry, 1995, Oct-31, Volume: 34, Issue:43

    Topics: Catalysis; Coenzymes; Deuterium; Electrons; Enterococcus; Hydrogen Peroxide; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Peroxidases

1995
Determination of the kinetic and chemical mechanism of malic enzyme using (2R,3R)-erythro-fluoromalate as a slow alternate substrate.
    Biochemistry, 1998, Dec-22, Volume: 37, Issue:51

    Topics: Animals; Carbon Isotopes; Catalysis; Cattle; Chickens; Coenzymes; Decarboxylation; Deuterium; Kinetics; Malate Dehydrogenase; Malates; NAD; NADP; Oxaloacetates; Rabbits; Substrate Specificity; Swine

1998