3-acetylpyridine adenine dinucleotide has been researched along with deuterium in 5 studies
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) |
---|---|---|---|---|---|
68 | 0 | 2 | 13,104 | 217 | 2,527 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 3 (60.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cleland, WW; Cook, PF; Gavva, SR; Harris, BG; Urbauer, JL; Weiss, PM | 1 |
Morrison, JF; Stone, SR | 1 |
Cleland, WW; Hermes, JD; Morrical, SW; O'Leary, MH | 1 |
Claiborne, A; Crane, EJ; Parsonage, D; Poole, LB | 1 |
Bradshaw, DE; Cleland, WW; Urbauer, JL | 1 |
5 other study(ies) available for 3-acetylpyridine adenine dinucleotide and deuterium
Article | Year |
---|---|
Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
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.
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.
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.
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.
Topics: Animals; Carbon Isotopes; Catalysis; Cattle; Chickens; Coenzymes; Decarboxylation; Deuterium; Kinetics; Malate Dehydrogenase; Malates; NAD; NADP; Oxaloacetates; Rabbits; Substrate Specificity; Swine | 1998 |