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Literature summary extracted from

  • Hou, Q.Q.; Sheng, X.; Wang, J.H.; Liu, Y.J.; Liu, C.B.
    QM/MM study of the mechanism of enzymatic limonene 1,2-epoxide hydrolysis (2012), Biochim. Biophys. Acta, 1824, 263-268 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.3.2.8 N55A site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type Rhodococcus erythropolis
3.3.2.8 R99K site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type Rhodococcus erythropolis
3.3.2.8 Y53F site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type Rhodococcus erythropolis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.3.2.8 cytosol
-
 Rhodococcus erythropolis 5829
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.3.2.8 limonene-1,2-epoxide + H2O Rhodococcus erythropolis
-
 limonene-1,2-diol
-
 ?
3.3.2.8 limonene-1,2-epoxide + H2O Rhodococcus erythropolis DCL14
-
 limonene-1,2-diol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.8 Rhodococcus erythropolis Q9ZAG3
-
-
3.3.2.8 Rhodococcus erythropolis DCL14 Q9ZAG3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
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 Rhodococcus erythropolis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.8 1-methylcyclohexene oxide + H2O
-
 Rhodococcus erythropolis 1-methylcyclohexane-1,2-diol
-
 ?
3.3.2.8 1-methylcyclohexene oxide + H2O
-
 Rhodococcus erythropolis DCL14 1-methylcyclohexane-1,2-diol
-
 ?
3.3.2.8 cyclohexene oxide + H2O
-
 Rhodococcus erythropolis cyclohexane-1,2-diol
-
 ?
3.3.2.8 cyclohexene oxide + H2O
-
 Rhodococcus erythropolis DCL14 cyclohexane-1,2-diol
-
 ?
3.3.2.8 indene oxide + H2O
-
 Rhodococcus erythropolis indane-1,2-diol
-
 ?
3.3.2.8 indene oxide + H2O
-
 Rhodococcus erythropolis DCL14 indane-1,2-diol
-
 ?
3.3.2.8 limonene-1,2-epoxide + H2O
-
 Rhodococcus erythropolis limonene-1,2-diol
-
 ?
3.3.2.8 limonene-1,2-epoxide + H2O
-
 Rhodococcus erythropolis DCL14 limonene-1,2-diol
-
 ?
3.3.2.8 additional information proposed hydrolysis mechanism, the Asp101-Arg99-Asp132 triad with a water molecule is regarded as the active central, overview Rhodococcus erythropolis ?
-
 ?
3.3.2.8 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

EC Number Subunits Comment Organism
3.3.2.8 dimer 2 * 16000, SDS-PAGE Rhodococcus erythropolis

Synonyms

EC Number Synonyms Comment Organism
3.3.2.8 LEH
-
 Rhodococcus erythropolis
3.3.2.8 limA
-
 Rhodococcus erythropolis
3.3.2.8 limonene 1,2-epoxide hydrolase
-
 Rhodococcus erythropolis

General Information

EC Number General Information Comment Organism
3.3.2.8 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
3.3.2.8 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