phosphonoacetic acid has been researched along with histidine in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (20.00) | 18.7374 |
| 1990's | 4 (80.00) | 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 |
|---|---|
| Cleland, WW; O'Leary, MH; Parmentier, LE; Schachman, HK; Turnbull, JL; Waldrop, GL | 1 |
| Schachman, HK; Wente, SR | 1 |
| Cunin, R; Hervé, G; Ladjimi, MM; Van Vliet, F; Xi, XG | 1 |
| Kleanthous, C; Schachman, HK; Wemmer, DE | 1 |
| Gao, L; Hwang, CB; Hwang, YT; Smith, JF | 1 |
5 other study(ies) available for phosphonoacetic acid and histidine
| Article | Year |
|---|---|
Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.
Topics: Alanine; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbon Isotopes; Catalysis; Histidine; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Macromolecular Substances; Models, Molecular; Mutation; Phosphonoacetic Acid; Recombinant Proteins; Structure-Activity Relationship; Succinates | 1992 |
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; DNA Mutational Analysis; Histidine; Lysine; Phosphonoacetic Acid; Structure-Activity Relationship | 1991 |
The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
Topics: Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Bacterial Proteins; Binding Sites; Carbamyl Phosphate; Catalysis; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Protein Binding; Substrate Specificity; Succinates; Succinic Acid | 1990 |
The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Succinates; Succinic Acid | 1988 |
Mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene can confer altered drug sensitivities.
Topics: Amino Acid Sequence; Animals; Antiviral Agents; Aphidicolin; Binding Sites; Chlorocebus aethiops; DNA-Directed DNA Polymerase; DNA, Viral; Drug Resistance, Microbial; Enzyme Inhibitors; Exodeoxyribonuclease V; Exodeoxyribonucleases; Genes, pol; Genes, Viral; Herpesvirus 1, Human; Histidine; Humans; Molecular Sequence Data; Mutation; Nucleosides; Open Reading Frames; Phosphonoacetic Acid; Protein Structure, Secondary; Recombination, Genetic; Tyrosine; Vero Cells; Viral Proteins | 1998 |