Protein Variants | Comment | Organism |
---|---|---|
N55A | site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type | Rhodococcus erythropolis |
R99K | site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type | Rhodococcus erythropolis |
Y53F | site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type | Rhodococcus erythropolis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Rhodococcus erythropolis | 5829 | - |
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 | 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 | Rhodococcus erythropolis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-methylcyclohexene oxide + H2O | - |
Rhodococcus erythropolis | 1-methylcyclohexane-1,2-diol | - |
? | |
1-methylcyclohexene oxide + H2O | - |
Rhodococcus erythropolis DCL14 | 1-methylcyclohexane-1,2-diol | - |
? | |
cyclohexene oxide + H2O | - |
Rhodococcus erythropolis | cyclohexane-1,2-diol | - |
? | |
cyclohexene oxide + H2O | - |
Rhodococcus erythropolis DCL14 | cyclohexane-1,2-diol | - |
? | |
indene oxide + H2O | - |
Rhodococcus erythropolis | indane-1,2-diol | - |
? | |
indene oxide + H2O | - |
Rhodococcus erythropolis DCL14 | indane-1,2-diol | - |
? | |
limonene-1,2-epoxide + H2O | - |
Rhodococcus erythropolis | limonene-1,2-diol | - |
? | |
limonene-1,2-epoxide + H2O | - |
Rhodococcus erythropolis DCL14 | limonene-1,2-diol | - |
? | |
additional information | proposed hydrolysis mechanism, the Asp101-Arg99-Asp132 triad with a water molecule is regarded as the active central, overview | Rhodococcus erythropolis | ? | - |
? | |
additional information | proposed hydrolysis mechanism, the Asp101-Arg99-Asp132 triad with a water molecule is regarded as the active central, overview | Rhodococcus erythropolis DCL14 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 16000, SDS-PAGE | Rhodococcus erythropolis |
Synonyms | Comment | Organism |
---|---|---|
LEH | - |
Rhodococcus erythropolis |
limA | - |
Rhodococcus erythropolis |
limonene 1,2-epoxide hydrolase | - |
Rhodococcus erythropolis |
General Information | Comment | Organism |
---|---|---|
additional information | reaction quantum mechanics/molecular mechanics (QM/MM) calculations, molecular dynamics simulations and active site structures of wild-type and mutant enzymes, overview. Rhodococcus erythropolis DCL14 LEH has the exceptionally low molecular mass of 16 kDa, which is too small to contain any of the highly conserved motifs of the catalytic triad used by alpha/beta-hydrolase folded EHs. LEH has a narrow substrate range compared to other EHs | Rhodococcus erythropolis |
physiological function | epoxide hydrolases (EHs) catalyze the hydrolysis of epoxides to vicinal diols. EHs are found in all types of living organisms, including mammals, invertebrates, plants, bacteria and fungi. They have three main functions: detoxification, metabolism, and synthesis of signaling molecules | Rhodococcus erythropolis |