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(-)-limonene oxide + H2O
(1R,2R,4S)-limonene-1,2-diol
-
-
-
?
(1R,2S)-1-methylcyclohexane oxide + H2O
(1S,2S)-1-methylcyclohexane-1,2-diol
-
-
-
ir
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1R,2S,4R)-limonene-1,2-diol
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
(1R,2S,4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
(1S,2R)-1-methylcyclohexane oxide + H2O
(1R,2R)-1-methylcyclohexane-1,2-diol
-
-
-
ir
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2R,4R)-limonene-1,2-diol
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
(1S,2R,4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1S2R4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
-
-
optically pure, diastereomeric excess above 99%
?
(4R)-limonene-1,2-epoxide + H2O
(4R)-limonene-1,2-diol
(4R)-limonene-1,2-epoxide + H2O
?
the mixture of cis (1R,2S,4R) and trans (1S,2R,4R) isomers of (+)-limonene-1,2-epoxide and the mixture of cis (1S,2R,4S) and trans (1R,2S,4S) isomers of (-)-limonene-1,2-epoxide are quantitatively converted into the diaxial (1S,2S,4R)- and (1R,2R,4S)-limonene-1,2-diols, respectively. Cyclopentene-1,2-epoxide is no substrate for enzyme CH55-LEH. Enzyme substrate specificity and stereospecificity, overview
-
-
?
(4S)-limonene-1,2-epoxide + H2O
(4S)-limonene-1,2-diol
(4S)-limonene-1,2-epoxide + H2O
?
the mixture of cis (1R,2S,4R) and trans (1S,2R,4R) isomers of (+)-limonene-1,2-epoxide and the mixture of cis (1S,2R,4S) and trans (1R,2S,4S) isomers of (-)-limonene-1,2-epoxide are quantitatively converted into the diaxial (1S,2S,4R)- and (1R,2R,4S)-limonene-1,2-diols, respectively. Cyclopentene-1,2-epoxide is no substrate for enzyme CH55-LEH. Enzyme substrate specificity and stereospecificity, overview
-
-
?
1,2-epoxy-2,6-dimethyl-5-heptene + H2O
(2S)-2,6-dimethyl-5-hepten-1,2-diol
-
-
-
?
1,2-epoxy-2-methyl-6-heptene + H2O
(2S)-2-methyl-6-heptene-1,2-diol
-
-
-
?
1,2-epoxy-2-methylheptane + H2O
(2S)-2-methylheptane-1,2-diol
-
-
-
?
1,2-epoxy-3-benzyl-2-methylpropane + H2O
(2S)-3-benzyl-2-methylpropane-1,2-diol
-
-
-
?
1-methylcyclohexene oxide + H2O
(1S,2S)-1-methylcyclohexane-1,2-diol
-
-
-
?
1-methylcyclohexene oxide + H2O
1-methylcyclohexane-1,2-diol
2 cyclohexene-1,2-epoxide + 2 H2O
(S,S)-cyclohexane-1,2-diol + (R,R)-cyclohexane-1,2-diol
2-butyloxirane + H2O
hexane-1,2-diol
4-(1-methylethenyl)-cyclohexan-1,2-epoxide + H2O
4-(1-methylethenyl)-cyclohexan-1,2-diol
-
-
-
?
cycloheptene-1,2-epoxide + H2O
cycloheptene-1,2-diol
cyclohexene oxide + H2O
(1S,2S)-trans cyclohexanediol + (1R,2R)-trans-cyclohexanediol
-
-
-
?
cyclohexene oxide + H2O
cyclohexane-1,2-diol
cyclohexene-1,2-epoxide + H2O
(R1,R2)-cyclohexane-1,2-diol
-
-
-
-
?
cyclohexene-1,2-epoxide + H2O
(S1,S2)-cyclohexane-1,2-diol
-
-
-
-
?
cyclohexene-1,2-epoxide + H2O
cyclohexane-1,2-diol
cyclopentene-1,2-epoxide + H2O
(R1,R2)-cyclopentane-1,2-diol
-
-
-
-
?
cyclopentene-1,2-epoxide + H2O
(S1,S2)-cyclopentane-1,2-diol
-
-
-
-
?
cyclopentene-1,2-epoxide + H2O
cyclopentane-1,2-diol
cyclopentene-oxide + H2O
(R,R)-cyclopentene-1,2-diol + (S,S)-cyclopentene-1,2-diol
indene oxide + H2O
indane-1,2-diol
limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
enantiomeric mixtures of (+)-limone oxide, overview. Enzyme CH55-LEH prefers the cis form of (-)-limonene oxide
-
-
?
limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
enantiomeric mixtures of (+)-limone oxide, overview. Enzyme Tomsk-LEH shows stereospecificity in the hydrolysis of cis/trans mixtures of (+)-limonene oxide by preferring the trans isomer
-
-
?
limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol + (1R,2R,4S)-limonene-1,2-diol
limonene-1,2-epoxide + H2O
limonene-1,2-diol
phenylethylenoxide + H2O
1-phenylethane-1,2-diol
rac-1-methyl-7-oxabicyclo[4.1.0]heptane + H2O
(1S,2S)-1-methylcyclohexane-1,2-diol + (1R,6S)-1-methyl-7-oxabicyclo[4.1.0]heptane
rac-2-(phenoxymethyl)oxirane + H2O
(2S)-2-(phenoxymethyl)oxirane + (2R)-3-phenoxypropane-1,2-diol
S-(-)-limonene + H2O
limonene-1,2-diol
styrene-7,8-oxide + H2O
styrene-7,8-diol
-
-
-
?
additional information
?
-
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1R,2S,4R)-limonene-1,2-diol
-
-
-
?
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1R,2S,4R)-limonene-1,2-diol
-
-
-
?
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
-
-
optically pure, diastereomeric excess above 99%
?
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1R,2S,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1R,2S,4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
-
-
optically pure, diastereomeric excess above 99%
?
(1R,2S,4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1R,2S,4S)-limonene-1,2-epoxide + H2O
(1R,2R,4S)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2R,4R)-limonene-1,2-diol
-
-
-
?
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2R,4R)-limonene-1,2-diol
-
-
-
?
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
-
-
optically pure, diastereomeric excess above 99%
?
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(1S,2R,4R)-limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol
the reaction mechanism involves epoxide protonation by Asp109, nucleophilic attack by water, and abstraction of a proton from water by Asp132. The isopropenyl group plays a crucial role because it restricts the half-chair conformation to one of the two possible helicities. In this conformation, attack on the different epoxide carbons will lead to either a chair-like or a twist-boat transition state structure, the latter resulting in a higher barrier. The regioselectivity is thus governed by conformational and not electronic factors
-
-
ir
(4R)-limonene-1,2-epoxide + H2O
(4R)-limonene-1,2-diol
-
-
-
?
(4R)-limonene-1,2-epoxide + H2O
(4R)-limonene-1,2-diol
-
-
-
?
(4S)-limonene-1,2-epoxide + H2O
(4S)-limonene-1,2-diol
-
-
-
?
(4S)-limonene-1,2-epoxide + H2O
(4S)-limonene-1,2-diol
-
-
-
?
1-methylcyclohexene oxide + H2O
1-methylcyclohexane-1,2-diol
-
-
-
?
1-methylcyclohexene oxide + H2O
1-methylcyclohexane-1,2-diol
-
-
-
?
2 cyclohexene-1,2-epoxide + 2 H2O
(S,S)-cyclohexane-1,2-diol + (R,R)-cyclohexane-1,2-diol
LEH is the catalyst in the hydrolytic desymmetrization of cyclohexene oxide with formation of (R,R)- and (S,S)-cyclohexene-1,2-diol. Wild-type LEH shows an enanioselectivity of 2% enantiomeric excess (S,S), analysis of (R,R)- and (S,S)-selective LEH mutant variants (80-94% enantiomeric excess)
-
-
?
2 cyclohexene-1,2-epoxide + 2 H2O
(S,S)-cyclohexane-1,2-diol + (R,R)-cyclohexane-1,2-diol
LEH is the catalyst in the hydrolytic desymmetrization of cyclohexene oxide with formation of (R,R)- and (S,S)-cyclohexene-1,2-diol. Wild-type LEH shows an enanioselectivity of 2% enantiomeric excess (S,S), analysis of (R,R)- and (S,S)-selective LEH mutant variants (80-94% enantiomeric excess)
-
-
?
2-butyloxirane + H2O
hexane-1,2-diol
-
-
-
?
2-butyloxirane + H2O
hexane-1,2-diol
-
-
-
?
cycloheptene-1,2-epoxide + H2O
cycloheptene-1,2-diol
-
-
-
?
cycloheptene-1,2-epoxide + H2O
cycloheptene-1,2-diol
-
-
-
?
cyclohexene oxide + H2O
cyclohexane-1,2-diol
-
-
-
?
cyclohexene oxide + H2O
cyclohexane-1,2-diol
-
-
-
?
cyclohexene-1,2-epoxide + H2O
cyclohexane-1,2-diol
-
-
-
?
cyclohexene-1,2-epoxide + H2O
cyclohexane-1,2-diol
0.25% activity compared to limonene-1,2-epoxide
-
-
?
cyclohexene-1,2-epoxide + H2O
cyclohexane-1,2-diol
0.25% activity compared to limonene-1,2-epoxide
-
-
?
cyclohexene-1,2-epoxide + H2O
cyclohexane-1,2-diol
-
-
-
?
cyclopentene-1,2-epoxide + H2O
cyclopentane-1,2-diol
low activity
-
-
?
cyclopentene-1,2-epoxide + H2O
cyclopentane-1,2-diol
low activity
-
-
?
cyclopentene-oxide + H2O
(R,R)-cyclopentene-1,2-diol + (S,S)-cyclopentene-1,2-diol
-
-
wild-type, 72% conversion, (R,R)-product with 14% enantiomeric excess
-
?
cyclopentene-oxide + H2O
(R,R)-cyclopentene-1,2-diol + (S,S)-cyclopentene-1,2-diol
-
-
wild-type, 72% conversion, (R,R)-product with 14% enantiomeric excess
-
?
indene oxide + H2O
indane-1,2-diol
-
-
-
?
indene oxide + H2O
indane-1,2-diol
-
-
-
?
indene oxide + H2O
indane-1,2-diol
-
-
-
?
limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol + (1R,2R,4S)-limonene-1,2-diol
enantiomeric mixtures of (+)-limone oxide, overview. Re-LEH catalyzes the quantitative conversion of the (+)- and (-)-limonene oxide cis/trans mixtures into the respective diols, the (+)-enantiomer is the better substrate
-
-
?
limonene-1,2-epoxide + H2O
(1S,2S,4R)-limonene-1,2-diol + (1R,2R,4S)-limonene-1,2-diol
enantiomeric mixtures of (+)-limone oxide, overview. Re-LEH catalyzes the quantitative conversion of the (+)- and (-)-limonene oxide cis/trans mixtures into the respective diols, the (+)-enantiomer is the better substrate
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
ir
limonene-1,2-epoxide + H2O
limonene-1,2-diol
part of limonene degradation pathway which allows the organism to grow on limone as sole source of carbon and energy
-
-
ir
limonene-1,2-epoxide + H2O
limonene-1,2-diol
limonene-1,2-epoxide is not the natural substrate of Tomsk-LEH
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
ir
limonene-1,2-epoxide + H2O
limonene-1,2-diol
part of limonene degradation pathway which allows the organism to grow on limone as sole source of carbon and energy
-
-
ir
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
-
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
limonene-1,2-epoxide is not the natural substrate of CH55-LEH
-
-
?
limonene-1,2-epoxide + H2O
limonene-1,2-diol
limonene-1,2-epoxide is not the natural substrate of Tomsk-LEH
-
-
?
phenylethylenoxide + H2O
1-phenylethane-1,2-diol
-
-
-
?
phenylethylenoxide + H2O
1-phenylethane-1,2-diol
-
-
-
?
rac-1-methyl-7-oxabicyclo[4.1.0]heptane + H2O
(1S,2S)-1-methylcyclohexane-1,2-diol + (1R,6S)-1-methyl-7-oxabicyclo[4.1.0]heptane
-
-
wild-type, 99% conversion, 19% enantiomeric excess for (1S,2S)-product
-
?
rac-1-methyl-7-oxabicyclo[4.1.0]heptane + H2O
(1S,2S)-1-methylcyclohexane-1,2-diol + (1R,6S)-1-methyl-7-oxabicyclo[4.1.0]heptane
-
-
wild-type, 99% conversion, 19% enantiomeric excess for (1S,2S)-product
-
?
rac-2-(phenoxymethyl)oxirane + H2O
(2S)-2-(phenoxymethyl)oxirane + (2R)-3-phenoxypropane-1,2-diol
-
-
wild-type, 33% conversion, 37% enantiomeric excess
-
?
rac-2-(phenoxymethyl)oxirane + H2O
(2S)-2-(phenoxymethyl)oxirane + (2R)-3-phenoxypropane-1,2-diol
-
-
wild-type, 33% conversion, 37% enantiomeric excess
-
?
S-(-)-limonene + H2O
limonene-1,2-diol
-
-
-
-
?
S-(-)-limonene + H2O
limonene-1,2-diol
-
-
-
-
?
additional information
?
-
commercially available cis/trans mixtures of (+)-limonene oxide (59:41 mixture of (1R,2S,4R) and (1S,2R,4R)) and (-)-limonene oxide (55:45 mixture of (1S,2R,4S) and (1R,2S,4S)) are dissolved in CH3CN and diluted with the appropriate LEH-containing buffer solution
-
-
?
additional information
?
-
enantioselectivity and activity of limonene epoxide hydrolase, overview
-
-
?
additional information
?
-
enzyme substrate specificity and stereospecificity, overview
-
-
?
additional information
?
-
-
enzyme substrate specificity and stereospecificity, overview
-
-
?
additional information
?
-
proposed hydrolysis mechanism, the Asp101-Arg99-Asp132 triad with a water molecule is regarded as the active central, overview
-
-
?
additional information
?
-
enantioselectivity and activity of limonene epoxide hydrolase, overview
-
-
?
additional information
?
-
proposed hydrolysis mechanism, the Asp101-Arg99-Asp132 triad with a water molecule is regarded as the active central, overview
-
-
?
additional information
?
-
commercially available cis/trans mixtures of (+)-limonene oxide (59:41 mixture of (1R,2S,4R) and (1S,2R,4R)) and (-)-limonene oxide (55:45 mixture of (1S,2R,4S) and (1R,2S,4S)) are dissolved in CH3CN and diluted with the appropriate LEH-containing buffer solution
-
-
?
additional information
?
-
commercially available cis/trans mixtures of (+)-limonene oxide (59:41 mixture of (1R,2S,4R) and (1S,2R,4R)) and (-)-limonene oxide (55:45 mixture of (1S,2R,4S) and (1R,2S,4S)) are dissolved in CH3CN and diluted with the appropriate LEH-containing buffer solution
-
-
?
additional information
?
-
commercially available cis/trans mixtures of (+)-limonene oxide (59:41 mixture of (1R,2S,4R) and (1S,2R,4R)) and (-)-limonene oxide (55:45 mixture of (1S,2R,4S) and (1R,2S,4S)) are dissolved in CH3CN and diluted with the appropriate LEH-containing buffer solution
-
-
?
additional information
?
-
-
stereochemistry and catalytic mechanism, overview
-
-
?
additional information
?
-
the mixture of cis (1R,2S,4R) and trans (1S,2R,4R) isomers of (+)-limonene-1,2-epoxide and the mixture of cis (1S,2R,4S) and trans (1R,2S,4S) isomers of (-)-limonene-1,2-epoxide are quantitatively converted into the diaxial (1S,2S,4R)- and (1R,2R,4S)-limonene-1,2-diols, respectively. Enzyme substrate specificity and stereospecificity, overview
-
-
?
additional information
?
-
the mixture of cis (1R,2S,4R) and trans (1S,2R,4R) isomers of (+)-limonene-1,2-epoxide and the mixture of cis (1S,2R,4S) and trans (1R,2S,4S) isomers of (-)-limonene-1,2-epoxide are quantitatively converted into the diaxial (1S,2S,4R)- and (1R,2R,4S)-limonene-1,2-diols, respectively. Enzyme substrate specificity and stereospecificity, overview
-
-
?
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malfunction
replacement of th catalytic aspartic acid residue to alanine (D82A) completely abolishes activity towards the tested substrates cyclohexene epoxide and (+)-limonene epoxide
malfunction
replacement of the catalytic aspartic acid residue to alanine (D80A) completely abolishes activity towards the tested substrates cyclohexene epoxide and (+)-limonene epoxide
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
physiological function
limonene-1,2-epoxide hydrolases (LEHs), a subset of the epoxide hydrolase family, present interesting opportunities for the mild, regio- and stereo- selective hydrolysis of epoxide substrates. LEHs show moderate enantioselectivity for non-natural ligands, combined with narrow substrate specificity
physiological function
-
limonene-1,2-epoxide hydrolases (LEHs), a subset of the epoxide hydrolase family, present interesting opportunities for the mild, regio- and stereo- selective hydrolysis of epoxide substrates. LEHs show moderate enantioselectivity for non-natural ligands, combined with narrow substrate specificity
-
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
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additional information
quantum mechanics/molecular mechanics (QM/MM) free energy calculations for the reaction with molecular dynamics simulations of the enzyme internal dynamics, and the calculation of binding affinities (using the WaterSwap method) for various representatives of the enzyme conformational ensemble, show that the presence of natural or non-natural substrates differentially modulates the dynamic and catalytic behavior of LEH. The cross-talk between the protein and the ligands favors the selection of specific substrate-dependent interactions in the binding site, priming reactive complexes to select different preferential reaction pathways. LEH substrate binding pocket structure, LEH forms a stable homodimer, and each monomer can bind a substrate molecule within its catalytic pocket, overview. Crucial role of monomer-monomer interactions in stabilizing and tuning LEH dynamics and stability. Hydrolysis by LEH occurs via a complex mechanism, the Asp101-Arg99-Asp132 triad drives a concerted reaction involving the deprotonation of a water molecule by Asp132, the nucleophilic attack of the resulting hydroxide ion on the epoxide and protonation of the oxirane ring by the protonated Asp101 (specifically labeled Ash101). Arg99 is strongly associated through hydrogen bonds and electrostatic interactions with both Asp101 and Asp132 and even if it is not directly involved in the reaction mechanism, its mutation results in a deactivated enzyme. This complex picture is completed by the proper positioning and activation of the nucleophilic water by the H-bond network formed by Asn55 and Tyr53 (and Asp132 itself). In the model, the side chains of the residues of the catalytic triad, the water molecule and the epoxide are included in the QM region. The opening of the epoxide can result from the attack on either of the two carbon atoms of the LEO oxirane ring. Experimental evidence indicates that the water molecule privileges the attack on the more substituted C1 atom
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
additional information
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structural and computational insight into the catalytic mechanism of limonene epoxide hydrolase variants in stereoselective transformations, molecular dynamics simulations
additional information
the enzyme's catalytic mechanism is different from that of the epoxide hydrolases, EHs, belonging to the alpha/beta-hydrolase superfamily. The LEH enzyme active site contains three residues (Asp101, Arg99, and Asp132) that act in a concerted fashion to activate a water molecule which is able to open the epoxide ring without the formation of a covalently bound alkyl-enzyme intermediate. Importance of the catalytic Asp80 residues for the enzymatic activity of Tomsk-LEH. The LEH substrate binding pocket appears to have high affinity for polar molecules and additional electron density is observed in the active site pocket in the different LEH structure. Active site structure, overview
additional information
the enzyme's catalytic mechanism is different from that of the epoxide hydrolases, EHs, belonging to the alpha/beta-hydrolase superfamily. The LEH enzyme active site contains three residues (Asp101, Arg99, and Asp132) that act in a concerted fashion to activate a water molecule which is able to open the epoxide ring without the formation of a covalently bound alkyl-enzyme intermediate. Importance of the catalytic Asp80 residues for the enzymatic activity of Tomsk-LEH. The LEH substrate binding pocket appears to have high affinity for polar molecules and additional electron density is observed in the active site pocket in the different LEH structure. Active site structure, overview
additional information
the enzyme's catalytic mechanism is different from that of the epoxide hydrolases, EHs, belonging to the alpha/beta-hydrolase superfamily. The LEH enzyme active site contains three residues (Asp101, Arg99, and Asp132) that act in a concerted fashion to activate a water molecule which is able to open the epoxide ring without the formation of a covalently bound alkyl-enzyme intermediate. Importance of the catalytic Asp82 residues for the enzymatic activity of CH55-LEH. The LEH substrate binding pocket appears to have high affinity for polar molecules and additional electron density is observed in the active site pocket in the different LEH structure. Active site structure, overview
additional information
the enzyme's catalytic mechanism is different from that of the epoxide hydrolases, EHs, belonging to the alpha/beta-hydrolase superfamily. The LEH enzyme active site contains three residues (Asp101, Arg99, and Asp132) that act in a concerted fashion to activate a water molecule which is able to open the epoxide ring without the formation of a covalently bound alkyl-enzyme intermediate. Importance of the catalytic Asp82 residues for the enzymatic activity of CH55-LEH. The LEH substrate binding pocket appears to have high affinity for polar molecules and additional electron density is observed in the active site pocket in the different LEH structure. Active site structure, overview
additional information
the N-terminal extension of Re-LEH involved in the intersubunit interface which increases the buried surface area. The LEH monomer fold contains a curved six-stranded mixed beta-sheet, with three alpha-helices packed onto its concave side to form the active site pocket. Active site structure, overview
additional information
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the N-terminal extension of Re-LEH involved in the intersubunit interface which increases the buried surface area. The LEH monomer fold contains a curved six-stranded mixed beta-sheet, with three alpha-helices packed onto its concave side to form the active site pocket. Active site structure, overview
additional information
-
quantum mechanics/molecular mechanics (QM/MM) free energy calculations for the reaction with molecular dynamics simulations of the enzyme internal dynamics, and the calculation of binding affinities (using the WaterSwap method) for various representatives of the enzyme conformational ensemble, show that the presence of natural or non-natural substrates differentially modulates the dynamic and catalytic behavior of LEH. The cross-talk between the protein and the ligands favors the selection of specific substrate-dependent interactions in the binding site, priming reactive complexes to select different preferential reaction pathways. LEH substrate binding pocket structure, LEH forms a stable homodimer, and each monomer can bind a substrate molecule within its catalytic pocket, overview. Crucial role of monomer-monomer interactions in stabilizing and tuning LEH dynamics and stability. Hydrolysis by LEH occurs via a complex mechanism, the Asp101-Arg99-Asp132 triad drives a concerted reaction involving the deprotonation of a water molecule by Asp132, the nucleophilic attack of the resulting hydroxide ion on the epoxide and protonation of the oxirane ring by the protonated Asp101 (specifically labeled Ash101). Arg99 is strongly associated through hydrogen bonds and electrostatic interactions with both Asp101 and Asp132 and even if it is not directly involved in the reaction mechanism, its mutation results in a deactivated enzyme. This complex picture is completed by the proper positioning and activation of the nucleophilic water by the H-bond network formed by Asn55 and Tyr53 (and Asp132 itself). In the model, the side chains of the residues of the catalytic triad, the water molecule and the epoxide are included in the QM region. The opening of the epoxide can result from the attack on either of the two carbon atoms of the LEO oxirane ring. Experimental evidence indicates that the water molecule privileges the attack on the more substituted C1 atom
-
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
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D101A
catalytically inactive, D101 is the acid catalyst that protonates the epoxide oxygen
D101N
catalytically inactive, D101 is the acid catalyst that protonates the epoxide oxygen
E45D/L74F/T76K/M78F/N92K/L114V/I116V
site-directed mutagenesis, the mutant lacking the N- and C-terminal mutations displays 86% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
I5C/S15P/A19K/T76K/E84C/T85V/G89C/S91C/N92K/Y96F/E124D
site-directed mutagenesis, the multisite mutant shows enhanced and inverted enantioselectivity, and an increase in apparent melting temperature relative to wild-type LEH from 50 to 85°C and a more than 250fold longer half-life
L114C/I116V
-
substrate cyclopentene-oxide, 72% conversion, (S,S)-product with 68% enantiomeric excess
L114I/I116V
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substrate cyclopentene-oxide, 74% conversion, (S,S)-product with 50% enantiomeric excess
L114V/I116V
-
substrate cyclopentene-oxide, 72% conversion, (S,S)-product with 60% enantiomeric excess
L74I/I80C
-
substrate cyclopentene-oxide, 75% conversion, (R,R)-product with 66% enantiomeric excess
L74I/I80V
-
substrate cyclopentene-oxide, 75% conversion, (R,R)-product with 58% enantiomeric excess
L74V/I80V
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substrate cyclopentene-oxide, 67% conversion, (R,R)-product with 53% enantiomeric excess
M32C/I80F/L114C/I116V
-
substrate rac-2-(phenoxymethyl)oxirane, 31% conversion, (2R)-product with 92% enantiomeric excess. Substrate rac-1-methyl-7-oxabicyclo[4.1.0]heptane, 99% conversion, (1S,2S)-product with 55% enantiomeric excess
M32L/L35C
-
substrate cyclopentene-oxide, 78% conversion, (S,S)-product with 16% enantiomeric excess
M32L/L35F
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substrate cyclopentene-oxide, 79% conversion, (S,S)-product with 24% enantiomeric excess
M32L/L35V
-
substrate cyclopentene-oxide, 78% conversion, (S,S)-product with 10% enantiomeric excess
M78F/V83I
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substrate cyclopentene-oxide, 82% conversion, (R,R)-product with 29% enantiomeric excess
M78I/V83I
-
substrate cyclopentene-oxide, 80% conversion, (R,R)-product with 13% enantiomeric excess
M78V/V83I
-
substrate cyclopentene-oxide, 68% conversion, (R,R)-product with 7% enantiomeric excess
N55D
catalytically inactive
N55D/D132N
catalytically inactive, folding correct
R99A
catalytically inactive
R99H
catalytically inactive
R99Q
catalytically inactive
S15P/A19K/E45K/T76K/T85V/N92K/Y96F/E124D
site-directed mutagenesis, the multisite mutant shows enhanced and inverted enantioselectivity, and an increase in apparent melting temperature relative to wild-type LEH from 50 to 85°C and a more than 250fold longer half-life, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 46°C and the enantiomeric excess is 80% in favor of (R,R)-cyclohexene-1,2-diol
S15P/M78F
site-directed mutagenesis, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 47°C and the enantiomeric excess is 34% in favor of (R,R)-cyclohexene-1,2-diol
S15P/M78F/N92K/F139V
site-directed mutagenesis, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 48°C and the enantiomeric excess is 39% in favor of (R,R)-cyclohexene-1,2-diol
S15P/M78F/N92K/F139V/T76K/T85K
site-directed mutagenesis, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 44°C and the enantiomeric excess is 45% in favor of (R,R)-cyclohexene-1,2-diol
S15P/M78F/N92K/F139V/T76K/T85K/E45D/I80V/E124D
site-directed mutagenesis, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 46°C and the enantiomeric excess is 80% in favor of (R,R)-cyclohexene-1,2-diol
T76D/L114V/I116V
site-directed mutagenesis, the mutant lacking the N- and C-terminal mutations, maintains enantioselectivity of 71% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
T76K/L114V/I116V
site-directed mutagenesis, the mutant lacking the N- and C-terminal mutations, maintains enantioselectivity of 71% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 44°C
T76K/L114V/I116V/F139V/L147F
site-directed mutagenesis, the mutant lacking the N-terminal mutations shows enantioselectivities of 82% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 45°C
T76K/L114V/I116V/N92D/F139V/L147F
site-directed mutagenesis, the mutant lacking the N-terminal mutations shows enantioselectivities of 82% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
T76K/L114V/I116V/N92K/F139V/L147F
site-directed mutagenesis, the mutant lacking the N-terminal mutations shows enantioselectivities of 83% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
T76K/L114V/I116V/N92K/F139V/L147F/S15D/A19K/L74F/M78F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 51°C, and the enantiomeric excess is 92% in favor of (S,S)-cyclohexene-1,2-diol
T76K/L114V/I116V/N92K/F139V/L147F/S15D/A19K/L74F/M78F/E45D
site-directed mutagenesis, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 51°C and the enantiomeric excess is 94% in favor of (S,S)-cyclohexene-1,2-diol
L74V/I80V
-
substrate cyclopentene-oxide, 67% conversion, (R,R)-product with 53% enantiomeric excess
-
M32L/L35C
-
substrate cyclopentene-oxide, 78% conversion, (S,S)-product with 16% enantiomeric excess
-
M32L/L35F
-
substrate cyclopentene-oxide, 79% conversion, (S,S)-product with 24% enantiomeric excess
-
M32L/L35V
-
substrate cyclopentene-oxide, 78% conversion, (S,S)-product with 10% enantiomeric excess
-
E45D/L74F/T76K/M78F/N92K/L114V/I116V
-
site-directed mutagenesis, the mutant lacking the N- and C-terminal mutations displays 86% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
-
I5C/S15P/A19K/T76K/E84C/T85V/G89C/S91C/N92K/Y96F/E124D
-
site-directed mutagenesis, the multisite mutant shows enhanced and inverted enantioselectivity, and an increase in apparent melting temperature relative to wild-type LEH from 50 to 85°C and a more than 250fold longer half-life
-
N55A
-
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
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R99K
-
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
-
S15P/A19K/E45K/T76K/T85V/N92K/Y96F/E124D
-
site-directed mutagenesis, the multisite mutant shows enhanced and inverted enantioselectivity, and an increase in apparent melting temperature relative to wild-type LEH from 50 to 85°C and a more than 250fold longer half-life, T50 30 (temperature at which 50% of enzyme activity is lost following a heat treatment for 30 min) is 46°C and the enantiomeric excess is 80% in favor of (R,R)-cyclohexene-1,2-diol
-
T76K/L114V/I116V/N92K/F139V/L147F
-
site-directed mutagenesis, the mutant lacking the N-terminal mutations shows enantioselectivities of 83% enantiomeric excess in favor of (S,S)-cyclohexene-1,2-diol
-
Y53F
-
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
-
D80A
site-directed mutagenesis, mutation of the catalytic residue, inactive mutant
D82A
site-directed mutagenesis, mutation of the catalytic residue, inactive mutant
I80Y/L114V/I116V
-
site-directed mutagenesis, mutant SZ348, no or poor activity with cyclohexene-1,2-epoxide
L74F/I80F/L114V/I116V/F139V
-
site-directed mutagenesis, mutant SZ718
L74F/M78F/I80F/L114V/I116V/F139V
-
site-directed mutagenesis, mutant SZ719
L74F/M78F/L103V/L114V/I116V/F139V/L147V
-
site-directed mutagenesis, mutant SZ92
L74F/M78V/I80V/L114F
-
site-directed mutagenesis, mutant SZ338, no activity with cyclohexene-1,2-epoxide
M32V/M78V/I80V/L114FM32V/M78V/I80V/L114F
-
site-directed mutagenesis, mutant SZ529
N55A
little residual activity
N55A
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
R99K
catalytically inactive
R99K
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
Y53F
partially active
Y53F
site-directed mutagenesis, QM/MM-optimized active structure of the enzyme mutant compared to wild-type
additional information
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application of directed evolution using iterative saturation mutagenesis as a means to engineer LEH mutants showing broad substrate scope with high stereoselectivity. Mutants are obtained which catalyze the desymmetrization of cyclopentene-oxide with stereoselective formation of either the (R,R)- or the (S,S)-diol on an optional basis. The mutants prove to be excellent catalysts for the desymmetrization of other meso-epoxides and for the hydrolytic kinetic resolution of racemic substrates
additional information
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes to obtain enantiomerically pure isomers, overview
additional information
mutations E45D, T76K, and N92K are located on or near the surface of LEH. It is likely that these mutations stabilize the protein by optimizing the distribution of charges on the enzyme surface, which is an established method of protein stabilization. Furthermore, S15D may form an ionic bond with A19K, thereby stabilizing a flexible N-terminal loop. Evolved thermostability-related mutations, structure-function relationships, overview
additional information
-
application of directed evolution using iterative saturation mutagenesis as a means to engineer LEH mutants showing broad substrate scope with high stereoselectivity. Mutants are obtained which catalyze the desymmetrization of cyclopentene-oxide with stereoselective formation of either the (R,R)- or the (S,S)-diol on an optional basis. The mutants prove to be excellent catalysts for the desymmetrization of other meso-epoxides and for the hydrolytic kinetic resolution of racemic substrates
-
additional information
-
mutations E45D, T76K, and N92K are located on or near the surface of LEH. It is likely that these mutations stabilize the protein by optimizing the distribution of charges on the enzyme surface, which is an established method of protein stabilization. Furthermore, S15D may form an ionic bond with A19K, thereby stabilizing a flexible N-terminal loop. Evolved thermostability-related mutations, structure-function relationships, overview
-
additional information
-
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes to obtain enantiomerically pure isomers, overview
-
additional information
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes, overview. The obtainment of the cis isomer from the same (+)-limonene oxide mixture by Tomsk-LEH-catalyzed resolution is not significantly improved
additional information
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes, overview. The obtainment of the cis isomer from the same (+)-limonene oxide mixture by Tomsk-LEH-catalyzed resolution is not significantly improved
additional information
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes, overview. The obtainment of the enantiomerically pure trans isomer, the increase of the reaction temperature to 50°C leads to an excellent resolution even at a substrate loading of 2 mol/l in reasonable reaction times
additional information
comparison of preparative resolution of (+)- and (-)-limonene oxide mixtures catalyzed by different LEHs under non-optimized conditions, optimization of the biocatalyzed processes, overview. The obtainment of the enantiomerically pure trans isomer, the increase of the reaction temperature to 50°C leads to an excellent resolution even at a substrate loading of 2 mol/l in reasonable reaction times
additional information
-
structural and computational insight into the catalytic mechanism of limonene epoxide hydrolase mutants in stereoselective transformations
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Van der Werf, M.J.; Orru, R.V.A.; Overkamp, K.M.; Swarts, H.J.; Ospiran, I.; Steinreiber, A.; de Bont, J.A.M.; Faber, K.
Substrate specificity and stereospecificity of limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14; an enzyme showing sequential and enantioconvergent substrate conversion
Appl. Microbiol. Biotechnol.
52
380-385
1999
Rhodococcus erythropolis
-
brenda
Barbirato, F.; Verdoes, J.C.; de Bont, J.A.M.; van der Werf, M.J.
The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases
FEBS Lett.
438
293-296
1998
Rhodococcus erythropolis
brenda
Van der Werf, M.J.; Overkamp, K.M.; de Bont, J.A.M.
Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolases
J. Bacteriol.
180
5052-5057
1998
Rhodococcus erythropolis
brenda
Arand, M.; Hallberg, B.M.; Zou, J.; Bergfors, T.; Oesch, F.; Van Der Werf, M.J.; De Bont, J.A.M.; Jones, T.A.; Mowbray, S.L.
Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
EMBO J.
22
2583-2592
2003
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis
brenda
Hopmann, K.H.; Hallberg, B.M.; Himo, F.
Catalytic mechanism of limonene epoxide hydrolase, a theoretical study
J. Am. Chem. Soc.
127
14339-14347
2005
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3), Rhodococcus erythropolis DCL14
brenda
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
Biochim. Biophys. Acta
1824
263-268
2011
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3)
brenda
Zheng, H.; Reetz, M.T.
Manipulating the stereoselectivity of limonene epoxide hydrolase by directed evolution based on iterative saturation mutagenesis
J. Am. Chem. Soc.
132
15744-15751
2010
Rhodococcus erythropolis, Rhodococcus erythropolis DCL 14
brenda
Molina, G.; Bution, M.L.; Bicas, J.L.; Dolder, M.A.; Pastore, G.M.
Comparative study of the bioconversion process using R-(+)- and S-(-)-limonene as substrates for Fusarium oxysporum 152B
Food Chem.
174
606-613
2015
Fusarium oxysporum, Fusarium oxysporum 152B
brenda
Li, G.; Zhang, H.; Sun, Z.; Liu, X.; Reetz, M.
Multiparameter optimization in directed evolution engineering thermostability, enantioselectivity, and activity of an epoxide hydrolase
ACS Catal.
6
3679-3687
2016
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3)
-
brenda
Rinaldi, S.; Van Der Kamp, M.; Ranaghan, K.; Mulholland, A.; Colombo, G.
Understanding complex mechanisms of enzyme reactivity the case of limonene-1,2-epoxide hydrolases
ACS Catal.
8
5698-5707
2018
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3)
-
brenda
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
Biochim. Biophys. Acta
1824
263-268
2012
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3)
brenda
Ferrandi, E.; Marchesi, C.; Annovazzi, C.; Riva, S.; Monti, D.; Wohlgemuth, R.
Efficient epoxide hydrolase catalyzed resolutions of (+)- and (-)-cis/trans-limonene oxides
ChemCatChem
7
3171-3178
2015
Rhodococcus erythropolis (Q9ZAG3), Rhodococcus erythropolis DCL14 (Q9ZAG3), uncultured organism (A0A0G3IAY2), uncultured organism (A0A0G3ICV8)
-
brenda
Ferrandi, E.E.; Sayer, C.; Isupov, M.N.; Annovazzi, C.; Marchesi, C.; Iacobone, G.; Peng, X.; Bonch-Osmolovskaya, E.; Wohlgemuth, R.; Littlechild, J.A.; Monti, D.
Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries
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282
2879-2894
2015
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brenda
Sun, Z.; Wu, L.; Bocola, M.; Chan, H.C.S.; Lonsdale, R.; Kong, X.D.; Yuan, S.; Zhou, J.; Reetz, M.T.
Structural and computational insight into the catalytic mechanism of limonene epoxide hydrolase mutants in stereoselective transformations
J. Am. Chem. Soc.
140
310-318
2018
uncultured organism
brenda