Crystallization (Comment) | Organism |
---|---|
modeling of substrate 1,2-epoxymenth-8-ene into the active site of crystal structure and evaluation of the roles of residues Arg99, Tyr53 and Asn55 by QM/MM-scannedenergy mapping | Rhodococcus erythropolis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
limonene-1,2-epoxide + H2O | Rhodococcus erythropolis | - |
limonene-1,2-diol | - |
? | |
limonene-1,2-epoxide + H2O | Rhodococcus erythropolis DCL14 | - |
limonene-1,2-diol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus erythropolis | Q9ZAG3 | - |
- |
Rhodococcus erythropolis DCL14 | Q9ZAG3 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 | Rhodococcus erythropolis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
limonene-1,2-epoxide + H2O | - |
Rhodococcus erythropolis | limonene-1,2-diol | - |
? | |
limonene-1,2-epoxide + H2O | - |
Rhodococcus erythropolis DCL14 | limonene-1,2-diol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LEH | - |
Rhodococcus erythropolis |
limonene 1,2-epoxide hydrolase | - |
Rhodococcus erythropolis |