EC Number   |
Reaction |
Reference |
|---|
   3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
catalytic mechanism analyzed by quantum mechanics/molecular mechanics (QM/MM) calculations, computational model, overview. Enzyme LEH reacts by a single-step concerted general acid-catalyzed mechanism, which is distinct from the two-step general base-catalyzed mechanism typical for the alpha/beta-hydrolase class of EHs. Overall, this mechanism is very similar to a borderline-SN2-type mechanism leading to nucleophilic attack at the more substituted oxirane carbon atom. Thus, no enzyme-substrate intermediate is detected during the experiments |
-, 752797 |
| 3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
catalytic mechanism, quantum mechanics/molecular mechanics (QM/MM) free energy calculations for the reaction with molecular dynamics simulations |
-, 752350 |
| 3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
catalyzes simultaneous sequential and enantioconvergent epoxide conversion |
208936 |
| 3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
LEH mechanism, substrate specificity and stereoselectivity |
753544 |
| 3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
mechanism involves a concerted general acid catalysis step involving the Asp101-Arg99-Asp132 triad. The water molecule acting as nucleophilic reagent moves to the more substituted oxirane carbon atom, its hydrogen atom transfers to Asp132, and hydroxyl attacks at C1. Meanwhile, Asp101 donates a proton to the epoxide oxygen opening the oxirane ring. This process has an energy barrier of 16.9 kcal/mol and an endothermicity of 8.2 kcal/mol, and yields (1R,2R,4S)-limonene-1,2-diol as product. Activation barriers of 16.9 and 25.1 kcal/mol are calculated at the B3LYP/6-31G(d,p)//CHARMM level for nucleophilic attack on the more and less substituted epoxide carbons, respectively |
-, 714359 |
| 3.3.2.8 | 1,2-epoxymenth-8-ene + H2O = menth-8-ene-1,2-diol |
one-step mechanism |
655334 |
