pyridoxamine phosphate has been researched along with histidine in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (100.00) | 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 |
---|---|
Hiromi, K; Kagamiyama, H; Kuramitsu, S; Morino, Y; Tanase, S; Yano, T | 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 |
3 other study(ies) available for pyridoxamine phosphate and histidine
Article | Year |
---|---|
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 |
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 |