pyridoxamine phosphate has been researched along with lysine in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (37.50) | 18.7374 |
| 1990's | 3 (37.50) | 18.2507 |
| 2000's | 1 (12.50) | 29.6817 |
| 2010's | 1 (12.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Christen, P; Finlayson, WL; Kirsch, JF; Kochhar, S | 1 |
| Dobryszycki, P; Kochman, M | 1 |
| Cook, PF; Kiick, DM | 1 |
| Gloss, LM; Kirsch, JF | 1 |
| Christen, P; Gehring, H; Jäger, J; Jansonius, JN; Malashkevich, VN; Sauder, U; Ziak, M | 1 |
| Ferramola de Sancovich, AM; Sancovich, HA; Sopena de Kracoff, YE | 1 |
| Conway, ME; Farber, GK; Hutson, SM; Yennawar, HP; Yennawar, NH | 1 |
| Brunzelle, JS; Bulfer, SL; Trievel, RC | 1 |
8 other study(ies) available for pyridoxamine phosphate and lysine
| Article | Year |
|---|---|
The stereospecific labilization of the C-4' pro-S hydrogen of pyridoxamine 5'-phosphate is abolished in (Lys258----Ala) aspartate aminotransferase.
Topics: Alanine; Aspartate Aminotransferases; Circular Dichroism; Escherichia coli; Lysine; Mutation; Pyridoxamine; X-Ray Diffraction | 1987 |
Fluorescence resonance energy transfer studies on the proximity between lysine-107 and cysteine-239 in rabbit muscle aldolase.
Topics: 4-Chloro-7-nitrobenzofurazan; Animals; Cysteine; Energy Transfer; Fructose-Bisphosphate Aldolase; Lysine; Muscles; Protein Binding; Protein Conformation; Pyridoxal Phosphate; Pyridoxamine; Rabbits; Spectrometry, Fluorescence | 1988 |
pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase.
Topics: Aspartate Aminotransferases; Aspartic Acid; Binding, Competitive; Dimethylformamide; Hydrogen-Ion Concentration; Ketoglutaric Acids; Kinetics; Lysine; Maleates; Myocardium; Pyridoxal Phosphate; Pyridoxamine; Temperature | 1983 |
Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
Topics: Aspartate Aminotransferases; Binding Sites; Cysteine; Escherichia coli; Imines; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Protein Conformation; Pyridoxal Phosphate; Pyridoxamine; Spectrophotometry; Structure-Activity Relationship; Titrimetry | 1995 |
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 |
Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase.
Topics: Animals; Enzyme Inhibitors; Kinetics; Levulinic Acids; Liver; Lysine; Models, Molecular; Porphobilinogen; Porphobilinogen Synthase; Pyridoxal Phosphate; Pyridoxamine; Pyruvates; Pyruvic Acid; Swine | 1995 |
Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms.
Topics: Alanine Transaminase; Binding Sites; Crystallization; Crystallography, X-Ray; Cysteine; D-Alanine Transaminase; Escherichia coli Proteins; Humans; Isoenzymes; Isoleucine; Lysine; Mitochondria; Models, Molecular; Oxo-Acid-Lyases; Protein Conformation; Protein Structure, Secondary; Pyridoxamine; Schiff Bases; Substrate Specificity; Transaminases; Valine | 2002 |
Crystal structure of Saccharomyces cerevisiae Aro8, a putative α-aminoadipate aminotransferase.
Topics: 2-Aminoadipate Transaminase; Catalytic Domain; Crystallography, X-Ray; HEPES; Humans; Lysine; Models, Molecular; Protein Structure, Tertiary; Pyridoxal Phosphate; Pyridoxamine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Substrate Specificity; Thermus thermophilus; Transaminases | 2013 |