3-deoxy-d-arabino-heptulosonate-7-phosphate has been researched along with nad in 2 studies
| Studies (3-deoxy-d-arabino-heptulosonate-7-phosphate) | Trials (3-deoxy-d-arabino-heptulosonate-7-phosphate) | Recent Studies (post-2010) (3-deoxy-d-arabino-heptulosonate-7-phosphate) | Studies (nad) | Trials (nad) | Recent Studies (post-2010) (nad) |
|---|---|---|---|---|---|
| 28 | 0 | 1 | 30,121 | 88 | 5,663 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (100.00) | 18.7374 |
| 1990's | 0 (0.00) | 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 |
|---|---|
| Bender, SL; Knowles, JR; Mehdi, S | 1 |
| Bender, SL; Knowles, JR; Widlanski, T | 1 |
2 other study(ies) available for 3-deoxy-d-arabino-heptulosonate-7-phosphate and nad
| Article | Year |
|---|---|
Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis.
Topics: Apoenzymes; Apoproteins; Bacterial Proteins; Catalysis; Cations, Divalent; Cobalt; Edetic Acid; Enzyme Activation; Escherichia coli; Kinetics; Lyases; NAD; Phosphorus-Oxygen Lyases; Spectrophotometry, Atomic; Sugar Phosphates | 1989 |
Dehydroquinate synthase: the use of substrate analogues to probe the early steps of the catalyzed reaction.
Topics: Catalysis; Deuterium; Kinetics; Lyases; Molecular Conformation; NAD; Oxidation-Reduction; Phosphorus-Oxygen Lyases; Substrate Specificity; Sugar Phosphates | 1989 |