EC Number   |
Reaction |
Reference |
|---|
    1.14.13.1 | salicylate + NADH + H+ + O2 = catechol + NAD+ + H2O + CO2 |
- |
- |
| 1.14.13.1 | salicylate + NADH + H+ + O2 = catechol + NAD+ + H2O + CO2 |
analysis of the reaction mechanism of SALH using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview. The whole enzymatic reaction contains two parts: the hydroxylation and decarboxylation. The deprotonated substrate is the active form, whereas the neutral form of salicylate corresponds to very a high energy barrier (39.8 kcal/mol) for the hydroxylation process, which is in line with the experimental result that the optimum pH is 7.6. The calculated results with the deprotonated substrate indicate that the hydroxylation and decarboxylation occur in a stepwise manner and the decarboxylation process is calculated to be the rate-limiting step with an energy barrier of 14.5 kal/mol. The catalytic reaction is highly exothermic. It proceeds via a C4a-hydorperoxyflavin |
-, 765851 |
| 1.14.13.1 | salicylate + NADH + H+ + O2 = catechol + NAD+ + H2O + CO2 |
oxidative decarboxylation of salicylate catalyzed by NahG, catalytic mechanism, detailed overview. The salicylate carboxyl group lies near a hydrophobic region that aids decarboxylation. A conserved histidine residue is proposed to assist the reaction by general base/general acid catalysis |
-, 764872 |
