4-nitrophenylgalactoside has been researched along with 2-nitrophenylgalactoside in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (25.00) | 18.2507 |
| 2000's | 4 (50.00) | 29.6817 |
| 2010's | 2 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cupples, CG; Huber, RE; Miller, JH | 1 |
| Amyes, TL; Heo, C; Huber, RE; Lin, S; Richard, JP | 1 |
| Hengstenberg, W; Schulte, D | 1 |
| Cheng, C; Cupples, CG; Edwards, RA; Hakda, S; Huber, RE | 1 |
| Dugdale, ML; Dymianiw, DL; Huber, RE; Kappelhoff, JC; Linton, LR; Liu, SY | 1 |
| Białkowska, AM; Cieśliński, H; Kur, J; Nowakowska, KM; Turkiewicz, M | 1 |
| Gänzle, MG; Schwab, C; Sørensen, KI | 1 |
| Fraser, ME; Huber, RE; Jancewicz, LJ; Lee, M; Sutendra, G; Wheatley, RW | 1 |
8 other study(ies) available for 4-nitrophenylgalactoside and 2-nitrophenylgalactoside
| Article | Year |
|---|---|
Determination of the roles of Glu-461 in beta-galactosidase (Escherichia coli) using site-specific mutagenesis.
Topics: beta-Galactosidase; Binding Sites; Drug Stability; Edetic Acid; Escherichia coli; Galactosidases; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Kinetics; Lactose; Mutation; Nitrophenylgalactosides; Ribose; Structure-Activity Relationship | 1990 |
Structure-reactivity relationships for beta-galactosidase (Escherichia coli, lac Z). 4. Mechanism for reaction of nucleophiles with the galactosyl-enzyme intermediates of E461G and E461Q beta-galactosidases.
Topics: Acetates; Azides; beta-Galactosidase; Escherichia coli; Formates; Galactose; Galactosides; Kinetics; Models, Chemical; Nitrophenylgalactosides; Point Mutation; Structure-Activity Relationship; Water | 1996 |
Engineering the active center of the 6-phospho-beta-galactosidase from Lactococcus lactis.
Topics: Amino Acid Substitution; Amino Acids; Bacterial Proteins; beta-Galactosidase; Binding Sites; Escherichia coli; Galactosephosphates; Glucosides; Glycoside Hydrolases; Lactococcus lactis; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Structure, Tertiary; Recombinant Fusion Proteins; Species Specificity; Substrate Specificity | 2000 |
Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer.
Topics: Amino Acid Substitution; beta-Galactosidase; Binding Sites; Binding, Competitive; Catalysis; Enzyme Activation; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Kinetics; Lac Operon; Lactose; Nitrophenylgalactosides; Protein Binding; Sequence Deletion; Thermodynamics; Tryptophan | 2003 |
Practical considerations when using temperature to obtain rate constants and activation thermodynamics of enzymes with two catalytic steps: native and N460T-beta-galactosidase (E. coli) as examples.
Topics: Algorithms; beta-Galactosidase; Biocatalysis; Escherichia coli; Escherichia coli Proteins; Hydrogen-Ion Concentration; Kinetics; Mutation; Nitrophenylgalactosides; Nonlinear Dynamics; Temperature; Thermodynamics | 2009 |
A new beta-galactosidase with a low temperature optimum isolated from the Antarctic Arthrobacter sp. 20B: gene cloning, purification and characterization.
Topics: Amino Acid Sequence; Antarctic Regions; Arthrobacter; beta-Galactosidase; Cloning, Molecular; Cold Temperature; DNA, Bacterial; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Genes, Bacterial; Genomic Library; Kinetics; Molecular Sequence Data; Molecular Weight; Nitrophenylgalactosides; RNA, Ribosomal, 16S; Sequence Alignment; Sequence Analysis, DNA; Substrate Specificity; Temperature | 2009 |
Heterologous expression of glycoside hydrolase family 2 and 42 β-galactosidases of lactic acid bacteria in Lactococcus lactis.
Topics: Bacterial Proteins; Cloning, Molecular; Enzyme Stability; Gene Expression; Glycoside Hydrolases; Hydrogen-Ion Concentration; Kinetics; Lactobacillus acidophilus; Lactobacillus plantarum; Lactococcus lactis; Lactose; Leuconostoc; Nitrophenylgalactosides; Recombinant Proteins; Streptococcus thermophilus; Substrate Specificity; Temperature | 2010 |
Ser-796 of β-galactosidase (Escherichia coli) plays a key role in maintaining a balance between the opened and closed conformations of the catalytically important active site loop.
Topics: Amino Acid Substitution; beta-Galactosidase; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isopropyl Thiogalactoside; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Nitrophenylgalactosides; Protein Conformation; Recombinant Proteins; Serine; Static Electricity | 2012 |