nitrophenylgalactosides has been researched along with histidine in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (40.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (20.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Jaffar, MB; Kumble, KD; Kumble, S | 1 |
| Artz, SW; Blum, PH; Holzschu, DL; Shand, RF; Urdea, MS | 1 |
| Kaback, HR; Püttner, IB | 1 |
| Huber, RE; Rob, B; Roth, NJ | 1 |
| Eibinger, M; Nidetzky, B; Schmölzer, K | 1 |
5 other study(ies) available for nitrophenylgalactosides and histidine
| Article | Year |
|---|---|
Inactivation of a beta-glucosidase from Arthrobotrys conoides by diethyl pyrocarbonate: evidence of histidine at the active site.
Topics: beta-Glucosidase; Binding Sites; Diethyl Pyrocarbonate; Histidine; Iodoacetamide; Mitosporic Fungi; Nitrophenylgalactosides; Pyridoxal Phosphate | 1992 |
Mutational analysis of the histidine operon promoter of Salmonella typhimurium.
Topics: Base Sequence; beta-Galactosidase; Chromosome Deletion; DNA Transposable Elements; Drug Resistance, Microbial; Genes, Bacterial; Genotype; Histidine; Molecular Sequence Data; Mutation; Nitrophenylgalactosides; Operon; Promoter Regions, Genetic; Salmonella typhimurium | 1989 |
lac permease of Escherichia coli containing a single histidine residue is fully functional.
Topics: Binding, Competitive; Biological Transport, Active; DNA Mutational Analysis; Escherichia coli; Escherichia coli Proteins; Ethylmaleimide; Histidine; Lactose; Membrane Transport Proteins; Monosaccharide Transport Proteins; Nitrophenylgalactosides; Structure-Activity Relationship; Symporters; Thiogalactosides | 1988 |
His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis.
Topics: beta-Galactosidase; Binding Sites; Catalysis; Chromatography, Thin Layer; Enzyme Activation; Enzyme Stability; Escherichia coli; Histidine; Hot Temperature; Hydrogen-Ion Concentration; Hydroxyl Radical; Kinetics; Magnesium; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Substrate Specificity | 1998 |
Active-Site His85 of Pasteurella dagmatis Sialyltransferase Facilitates Productive Sialyl Transfer and So Prevents Futile Hydrolysis of CMP-Neu5Ac.
Topics: Asparagine; Catalytic Domain; Cytidine Monophosphate; Glycosylation; Histidine; Hydrolysis; Kinetics; Lactose; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Pasteurella; Point Mutation; Sialic Acids; Sialyltransferases; Water | 2017 |