shikimic acid-3-phosphate has been researched along with lysine in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (33.33) | 18.7374 |
| 1990's | 3 (50.00) | 18.2507 |
| 2000's | 1 (16.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Huynh, QK | 1 |
| Bauer, SC; Bild, GS; Borgmeyer, JR; Huynh, QK; Kishore, GM | 1 |
| Bild, GS; Huynh, QK; Kishore, GM | 1 |
| Ahmad, S; Arora, N; Bhatnagar, RK; Fattah, FA; Majumder, K; Selvapandiyan, A | 1 |
| Cohen, ER; McDowell, LM; Schaefer, J; Schmidt, A; Studelska, DR | 1 |
| Berti, PJ; Chindemi, P | 1 |
6 other study(ies) available for shikimic acid-3-phosphate and lysine
| Article | Year |
|---|---|
5-Enolpyruvylshikimate-3-phosphate synthase from Escherichia coli--the substrate analogue bromopyruvate inactivates the enzyme by modifying Cys-408 and Lys-411.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Amino Acid Sequence; Cysteine; Enzyme Activation; Escherichia coli; Hydrolysis; Kinetics; Ligands; Lysine; Molecular Sequence Data; Pyruvates; Shikimic Acid; Substrate Specificity; Transferases; Trypsin | 1991 |
Site-directed mutagenesis of Petunia hybrida 5-enolpyruvylshikimate-3-phosphate synthase: Lys-23 is essential for substrate binding.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alanine; Alkyl and Aryl Transferases; Arginine; Binding Sites; Binding, Competitive; Glutamates; Glutamic Acid; Glycine; Glyphosate; Herbicides; Lysine; Mutation; Phosphoenolpyruvate; Plants; Pyridoxal Phosphate; Shikimic Acid; Transferases | 1988 |
5-Enolpyruvyl shikimate 3-phosphate synthase from Escherichia coli. Identification of Lys-22 as a potential active site residue.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Amino Acid Sequence; Binding Sites; Chromatography, High Pressure Liquid; Escherichia coli; Kinetics; Lysine; Peptide Fragments; Phosphoenolpyruvate; Shikimic Acid; Transferases; Trypsin | 1988 |
Point mutation of a conserved arginine (104) to lysine introduces hypersensitivity to inhibition by glyphosate in the 5-enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Amino Acid Sequence; Arginine; Bacillus subtilis; Binding Sites; Conserved Sequence; Enzyme Inhibitors; Glutamine; Glycine; Glyphosate; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phosphoenolpyruvate; Point Mutation; Shikimic Acid; Substrate Specificity; Transferases | 1995 |
Structural constraints on the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Alkyl and Aryl Transferases; Arginine; Binding Sites; Escherichia coli; Glycine; Glyphosate; Histidine; Lysine; Magnetic Resonance Spectroscopy; Molecular Structure; Nitrogen Isotopes; Shikimic Acid; Transferases | 1996 |
Catalytic residues and an electrostatic sandwich that promote enolpyruvyl shikimate 3-phosphate synthase (AroA) catalysis.
Topics: 3-Phosphoshikimate 1-Carboxyvinyltransferase; Aspartic Acid; Catalysis; Catalytic Domain; Cations; Crystallography, X-Ray; Enzyme Stability; Escherichia coli Proteins; Glutamates; Kinetics; Lysine; Shikimic Acid; Static Electricity; Streptococcus pneumoniae; Substrate Specificity | 2009 |