EC Number   |
Reaction |
Reference |
|---|
   3.1.1.7 | acetylcholine + H2O = choline + acetate |
- |
- |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
computer-modelled comparison of ordered uni bi and ki kinetic mechanism. ki model is accurate at equilibrium and when the inhibitor concentration is well below its Kd value |
666972 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
formation of the trigonal bipyramidal transition state |
678274 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
mathematical modelling of mechanism |
664186 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
mechanism |
650215, 651586 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
reaction mechanism, active site structure, the catalytic triad comprises the residues Ser203, His447, Glu334, residues Ser203 and His447 are directly involved in the reaction, serving as nucleophilic attacking group and general acid base catalytic elements, respectively, at the acylation stage of the enzymatic reaction. Modern molecular modeling using tools including molecular docking, molecular dynamics (MD), quantum chemistry and the combined quantum mechanical-molecular mechanical method, overview |
693706 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
reaction mechanism, structure-function relationship analysis, binding structure and mechanism of substrate and product at both the peripheral and active sites, overview |
679488 |
| 3.1.1.7 | acetylcholine + H2O = choline + acetate |
the mechanism for AChE-catalyzed hydrolysis of substrate is formation of the first tetrahedral intermediate via nucleophilic attack of the active site serine |
708139 |
