aspartic acid has been researched along with n-methylhydroxylamine in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 1 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brzović, PS; Dunn, MF; Kayastha, AM; Miles, EW | 1 |
| Dunn, MF; Ferrari, D; Miles, EW; Yang, LH | 1 |
2 other study(ies) available for aspartic acid and n-methylhydroxylamine
| Article | Year |
|---|---|
Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium.
Topics: Aspartic Acid; Base Sequence; Binding Sites; Catalysis; Glutamates; Glutamic Acid; Hydroxylamines; Molecular Sequence Data; Mutagenesis, Site-Directed; Salmonella typhimurium; Serine; Spectrophotometry; Substrate Specificity; Tryptophan; Tryptophan Synthase | 1992 |
Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.
Topics: Alanine; Allosteric Regulation; Aniline Compounds; Aspartic Acid; Benzimidazoles; beta-Alanine; Catalysis; Deuterium; Enzyme Activation; Hydroxylamines; Indoles; Kinetics; Multienzyme Complexes; Mutagenesis, Site-Directed; Pyruvic Acid; Salmonella typhimurium; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Substrate Specificity; Titrimetry; Tryptophan Synthase | 2001 |