deuterium has been researched along with dihydroxyacetone phosphate in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 5 (55.56) | 18.7374 |
| 1990's | 3 (33.33) | 18.2507 |
| 2000's | 1 (11.11) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Albery, WJ; Knowles, JR; Leadlay, PF | 1 |
| Albery, WJ; Fisher, LM; Knowles, JR | 1 |
| Knowles, JR; Nickbarg, EB | 1 |
| Kadonaga, JT; Knowles, JR | 1 |
| Iyengar, R; Rose, IA | 1 |
| Alston, WC; Kanska, M; Murray, CJ | 1 |
| Cole, RN; Comer, FI; Harris, TK; Mildvan, AS | 1 |
| Sampson, NS; Sun, J | 1 |
| Bates, MA; Berry, A; Plater, AR; Thomson, GJ; Zgiby, S | 1 |
9 other study(ies) available for deuterium and dihydroxyacetone phosphate
| Article | Year |
|---|---|
Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reaction.
Topics: Carbohydrate Epimerases; Deuterium; Dihydroxyacetone Phosphate; Glyceraldehyde; Kinetics; Protons; Triose-Phosphate Isomerase; Trioses | 1976 |
Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent water.
Topics: Carbohydrate Epimerases; Deuterium; Dihydroxyacetone Phosphate; Glyceraldehyde; Kinetics; Mass Spectrometry; Protons; Triose-Phosphate Isomerase; Trioses | 1976 |
Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli.
Topics: Animals; Carbohydrate Epimerases; Chickens; Cloning, Molecular; Deuterium; Dihydroxyacetone Phosphate; Energy Metabolism; Escherichia coli; Kinetics; Saccharomyces cerevisiae; Thermodynamics; Triose-Phosphate Isomerase; Tritium | 1988 |
Role of mono- and divalent metal cations in the catalysis by yeast aldolase.
Topics: Deuterium; Dihydroxyacetone Phosphate; Fructose-Bisphosphate Aldolase; Mathematics; Metals; Models, Chemical; Potassium; Saccharomyces cerevisiae | 1983 |
Partition of intermediates of triosephosphate isomerase: slow conformational changes precede enolization and follow product release.
Topics: Animals; Carbohydrate Epimerases; Chemical Phenomena; Chemistry; Chickens; Deuterium; Dihydroxyacetone Phosphate; Geobacillus stearothermophilus; Glyceraldehyde; Glyceraldehyde 3-Phosphate; Kinetics; Muscles; Protein Conformation; Rabbits; Saccharomyces cerevisiae; Triose-Phosphate Isomerase; Trioses; Tritium | 1982 |
Secondary H/T and D/T isotope effects in enzymatic enolization reactions. Coupled motion and tunneling in the triosephosphate isomerase reaction.
Topics: Animals; Binding Sites; Deuterium; Dihydroxyacetone Phosphate; Fungal Proteins; Glyceraldehyde 3-Phosphate; Hydrogen; Kinetics; Models, Chemical; Molecular Conformation; Molecular Structure; Muscles; Rabbits; Thermodynamics; Triose-Phosphate Isomerase; Tritium | 1996 |
Proton transfer in the mechanism of triosephosphate isomerase.
Topics: Animals; Deuterium; Dihydroxyacetone Phosphate; Electron Transport; Glyceraldehyde 3-Phosphate; Muscle, Skeletal; Protons; Rabbits; Substrate Specificity; Temperature; Triose-Phosphate Isomerase; Tritium | 1998 |
Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase.
Topics: Animals; Binding Sites; Chickens; Deuterium; Dihydroxyacetone Phosphate; Hot Temperature; Kinetics; Models, Molecular; Multigene Family; Mutagenesis, Insertional; Peptide Fragments; Protein Conformation; Protein Denaturation; Structure-Activity Relationship; Triose-Phosphate Isomerase | 1999 |
A functional role for a flexible loop containing Glu182 in the class II fructose-1,6-bisphosphate aldolase from Escherichia coli.
Topics: Amino Acid Substitution; Binding Sites; Catalysis; Circular Dichroism; Deuterium; Dihydroxyacetone Phosphate; Escherichia coli; Fructose-Bisphosphate Aldolase; Glutamic Acid; Hydroxamic Acids; Kinetics; Models, Molecular; Oxidation-Reduction; Pliability; Protein Conformation; Protons; Structure-Activity Relationship; Zinc | 2002 |