histidine has been researched along with pyridoxamine in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (57.14) | 18.7374 |
| 1990's | 3 (42.86) | 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 |
|---|---|
| Gibbons, I; Ritchey, JM; Schachman, HK | 1 |
| Hiromi, K; Kagamiyama, H; Kuramitsu, S; Morino, Y; Tanase, S; Yano, T | 1 |
| Albritton, WL; Levin, AP | 1 |
| Cheng, S; Martinez-Carrion, M; Relimpio, AM | 1 |
| Bhagwat, AS; McFadden, BA | 1 |
| Christen, P; Gehring, H; Jäger, J; Jansonius, JN; Malashkevich, VN; Sauder, U; Ziak, M | 1 |
| Christen, P; Jansonius, JN; Malashkevich, VN; Sandmeier, E; Vacca, RA | 1 |
7 other study(ies) available for histidine and pyridoxamine
| Article | Year |
|---|---|
Reactivation of enzymes by light-stimulated cleavage of reduced pyridoxal 5'-phosphate-enzyme complexes.
Topics: Aspartate Carbamoyltransferase; Enzyme Activation; Histidine; Hydrogen-Ion Concentration; Kinetics; L-Serine Dehydratase; Lyases; Lysine; Magnetic Resonance Spectroscopy; Molecular Weight; Photolysis; Protein Binding; Pyridoxal Phosphate; Pyridoxamine; Tryptophanase; Tyrosine; Ultraviolet Rays | 1977 |
The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.
Topics: Aspartate Aminotransferases; Base Sequence; Binding Sites; Catalysis; Circular Dichroism; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Pyridoxal Phosphate; Pyridoxamine; Spectrophotometry, Ultraviolet | 1991 |
Aminotransferase from a deletion mutant in the histidine operon.
Topics: Amino Acids; Autoanalysis; Catalysis; Cell-Free System; Centrifugation, Density Gradient; Chromatography, Ion Exchange; Chromosome Mapping; Coenzymes; Genetics, Microbial; Glutamates; Histidine; Hot Temperature; Imidazoles; Immunochemistry; Molecular Weight; Mutation; Operon; Pyridoxal; Pyridoxamine; Salmonella typhimurium; Spectrum Analysis; Transaminases | 1972 |
Nuclear magnetic resonance of aspartate transaminase. A 19 F and 1 H investigation of the binding of dicarboxylic acids to various forms of each isoenzyme.
Topics: Animals; Apoproteins; Aspartate Aminotransferases; Binding Sites; Binding, Competitive; Dicarboxylic Acids; Fluorine; Glutamates; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Magnetic Resonance Spectroscopy; Mitochondria, Muscle; Models, Chemical; Myocardium; Pyridoxal; Pyridoxal Phosphate; Pyridoxamine; Structure-Activity Relationship; Subcellular Fractions; Succinates; Swine | 1973 |
Pyridoxal phosphate as a probe in the active site of ribulose bisphosphate carboxylase/oxygenase.
Topics: Binding Sites; Carboxy-Lyases; Electrophoresis, Polyacrylamide Gel; Histidine; Lysine; Oxidation-Reduction; Photochemistry; Plants; Pyridoxal Phosphate; Pyridoxamine; Ribulose-Bisphosphate Carboxylase; Spectrum Analysis | 1983 |
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Topics: Animals; Aspartate Aminotransferases; Binding Sites; Catalysis; Chickens; Crystallography, X-Ray; Escherichia coli; Histidine; Ketoglutaric Acids; Lysine; Protein Binding; Pyridoxal Phosphate; Pyridoxamine; Structure-Activity Relationship; Substrate Specificity | 1995 |
Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
Topics: Animals; Aspartate Aminotransferases; Base Sequence; Catalysis; Chickens; Crystallography, X-Ray; Escherichia coli; Histidine; Kinetics; Molecular Sequence Data; Mutation; Oligodeoxyribonucleotides; Pyridoxamine; Substrate Specificity | 1995 |