EC Number   |
Inhibitors  |
Structure |
|---|
    1.1.1.3 | more |
enzyme is not inhibited by other aspartate-derived amino acids than threonine |
 |
| 1.1.1.3 | more |
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine |
|
| 1.1.1.3 | more |
inhibitor docking study, overview |
|
| 1.1.1.3 | more |
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory |
|
| 1.1.1.3 | more |
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory |
|
| 1.1.1.3 | more |
L-homoserine inhibits the activity of aspartokinase encoded by metL |
|
| 1.1.1.3 | more |
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine |
|
| 1.1.1.3 | more |
PbHSD inhibitor screening using the Zinc library, molecular dynamics simulations of PbHSD and ligand docking, electrostatic contacts between protein residues and the respective ligand atoms, overview. The selected ligands remain bound to the protein by a common mechanism throughout the simulation. Cytotoxicity evaluation in HeLa and Vero cells |
|
| 1.1.1.3 | more |
tHSD is poorly inhibited by less than 5% by 10 mM L-methionine, L-isoleucine, or L-threonine, all of which are final products in the aspartate pathway, and by L-lysine |
|
| 1.1.1.3 | NADH |
acts as a competitive inhibitor of NAD+, product inhibition, non-competitive inhibition versus L-homoserine |
  |
