3.3.2.8: limonene-1,2-epoxide hydrolase
This is an abbreviated version!
For detailed information about limonene-1,2-epoxide hydrolase, go to the full flat file.
Word Map on EC 3.3.2.8
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3.3.2.8
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stereoselective
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rhodococcus
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erythropolis
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hydrolases
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desymmetrization
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cyclohexene
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enantioselective
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alphabet
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regioselective
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lining
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six-stranded
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astronomically
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intricacies
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valpromide
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selenomethionine-substituted
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biocatalysis
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single-wavelength
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wide-ranging
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diols
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polyketide
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cyclopentene
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synthesis
- 3.3.2.8
-
stereoselective
- rhodococcus
- erythropolis
- hydrolases
-
desymmetrization
- cyclohexene
-
enantioselective
-
alphabet
-
regioselective
-
lining
-
six-stranded
-
astronomically
-
intricacies
- valpromide
-
selenomethionine-substituted
-
biocatalysis
-
single-wavelength
-
wide-ranging
- diols
- polyketide
-
cyclopentene
- synthesis
Reaction
Synonyms
CH55-LEH, LEH, limA, limonene 1,2-epoxide hydrolase, limonene epoxide hydrolase, limonene oxide hydrolase, limonene-1,2-epoxide hydrolase, Re-LEH, Tomsk-LEH
ECTree
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Crystallization
Crystallization on EC 3.3.2.8 - limonene-1,2-epoxide hydrolase
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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
purified enzyme mutant H-2-H5 (E45D/L74F/T76K/M78F/N92K/L114V/I116V) and mutant H-2-H5 in complex with (S,S)-cyclohexenediol, sitting-drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM potassium phosphate buffer, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 2% v/v PEG 400, and 2.0 M ammonium sulfate, and equilibration against reservoir solution, 20°C, the single protein crystals are soaked in 100 mM ligand solution for 1 min, X-ray diffraction structure determination and analysis, molecular replacement method using the wild-type LEH (PDB ID 1NU3) as a search model, comparison of crystal structures of wild-type and mutant enzymes
mutant SZ348, sitting-drop vapor diffusion method, crystallized in 2.4 M sodium/potassium phosphate, 0.1 M Tris-HCl, pH 8.5, mixing of 0.002 ml of 16 mg/ml protein solution with 0.002 ml of reservoir solution, equilibration against the reservoir solution. The complex crystals of SZ348-CYO1 are made by soaking the crystals of SZ348 in sodium/potassium phosphate, 0.1 M Tris-HCl, pH 8.5, 10 mM of cyclopentene-1,2-epoxide, and 2.5% v/v acetonitrile for 5-10 min, at 18°C, X-ray diffraction structure determination and analysis
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purified recombinant enzyme in apoform or in complex with inhibitor poly(ethylene glycol), 10 mg/ml protein solution is mixed with an equal volume of precipitant solution and is covered with a 1:1 mix of silicon and paraffin oils, X-ray diffraction structure determination and analysis at 1.42-1.47 A resolution
purified recombinant enzyme in apoform or in complex with inhibitor valpromide, 10 mg/ml protein solution is mixed with an equal volume of precipitant solution and is covered with a 1:1 mix of silicon and paraffin oils, X-ray diffraction structure determination and analysis at 1.16-1.26 A resolution