EC Number   |
Reaction |
Reference |
|---|
   3.1.1.8 | an acylcholine + H2O = choline + a carboxylate |
enzyme is able to stabilize covalent tetrahedral intermediate adduct with substrate |
665304 |
| 3.1.1.8 | an acylcholine + H2O = choline + a carboxylate |
mechanism |
651156, 651593, 94445 |
| 3.1.1.8 | an acylcholine + H2O = choline + a carboxylate |
molecular dynamics simulation in aqueous solution, nucleophilic S198 and the various binding subsites in the catalytic cavitiy are readily accessible from the exterior of the protein, the catalytic triad E325/H438/S198 is stablized by presence of a sodium ion |
666874 |
| 3.1.1.8 | an acylcholine + H2O = choline + a carboxylate |
the catalytic residue is Ser198 |
678453 |
| 3.1.1.8 | an acylcholine + H2O = choline + a carboxylate |
the enzyme follows a mechanism similar to that of a serine protease in which the activated serine attacks the acyl-substrate to form an acyl-enzyme intermediate. The acyl-enzyme intermediate then reacts directly with a water molecule at the active site. Both the acylation and deacylation reactions occur through a tetrahedral intermediate |
750017 |
