deuterium has been researched along with dehydroalanine in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (66.67) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cook, PF; Kim, SK; Kredich, NM; Nalabolu, SR; Rege, VD; Schnackerz, KD; Tai, CH; Yoon, MY | 1 |
| Jemielity, J; Kańska, M; Lewandowicz, A; Paneth, P; Zoń, J | 1 |
| Cook, PF; Daum, S; Tai, CH | 1 |
3 other study(ies) available for deuterium and dehydroalanine
| Article | Year |
|---|---|
Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.
Topics: Alanine; Binding Sites; Circular Dichroism; Cysteine; Cysteine Synthase; Deuterium; Enzyme Activation; Enzyme Stability; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Mutagenesis, Insertional; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet | 1998 |
Tritium secondary kinetic isotope effect on phenylalanine ammonia-lyase-catalyzed reaction.
Topics: Alanine; Catalytic Domain; Deuterium; Kinetics; Models, Chemical; Phenylalanine Ammonia-Lyase; Rhodotorula; Substrate Specificity; Tritium | 1999 |
Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction.
Topics: Alanine; Aspartic Acid; Binding Sites; Catalysis; Circular Dichroism; Cysteine Synthase; Deuterium; Hydrogen Bonding; Kinetics; Mutagenesis, Site-Directed; Pyridines; Pyridoxal Phosphate; Serine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Substrate Specificity | 2003 |