EC Number   |
Reaction |
Reference |
|---|
    3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate |
active site serine residue |
646199 |
| 3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate |
based on the results of quantum mechanics/molecular mechanics metadynamics techniques simulations, it is demonstrated that hotdog-fold hTHEM2 follows a simple mechanism in which a water molecule directly attacks the carbonyl carbon atom to cleave the thioester bond without requiring an enzyme-substrate covalent intermediate the reaction, providing evidence for the formation of a tetrahedral-like transition state |
731658 |
| 3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate |
catalytic triad D233-S255-Q305 |
646200 |
| 3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate |
catalytic triad D337-Q409-S359 |
646195 |
| 3.1.2.20 | an acyl-CoA + H2O = CoA + a carboxylate |
molecular dynamics studies show that certain residues of the substrate binding tunnel are flexibel and thus modulate the length of the tunnel |
732194 |
