Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.3.2.10: soluble epoxide hydrolase

This is an abbreviated version!
For detailed information about soluble epoxide hydrolase, go to the full flat file.

Word Map on EC 3.3.2.10

Reaction

an epoxide
+
H2O
=
a glycol

Synonyms

AnEH, BNSEH1, CEH, Cterm-EH, Cytosolic epoxide hydrolase, EC 3.1.3.76, EC 3.3.2.3, EC 4.2.1.63, EC 4.2.1.64, EET-metabolizing enzyme, EH, EH3, EPHX2, EPHX3, epoxide hydrolase 1, epoxide hydrolase 2, epoxide hydrolase-3, epoxyeicosatrienonic acid-metabolizing enzyme, EPXH1, EPXH2, EPXH2B, hepoxilin hydrolase, hsEH, mEH, More, PNSO hydrolase, PsEH, s-EH, SEH, soluble epoxide hydrolase, soluble-type epoxide hydrolase, SPEH1, SPEH2, TESO hydrolase, TSO hydrolase

ECTree

     3 Hydrolases
         3.3 Acting on ether bonds
             3.3.2 Ether hydrolases
                3.3.2.10 soluble epoxide hydrolase

Crystallization

Crystallization on EC 3.3.2.10 - soluble epoxide hydrolase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method
-
three-dimensional crystal structure is determined at 3.5 A resolution by the multiwavelength anomalous diffraction method using crystals of a seleno-methionine substituted form of enzyme and then refined at 1.8 A resolution
hanging drop vapor diffusion method, using 30% (w/v) PEG 3350, 0-10% (w/v) sucrose, at 4°C
His-tagged hydrolase domain, in complex with inhibitor N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyclopentylacetamide. The compound binds deeply within the active site of sEH, forming a network of hydrogen-bonding interactionswith key protein atoms
modeling of structure in complex with inhibitor N-(1-trifluoroacetylpiperidin-4-yl)-N'-(adamant-1-yl) urea
purified recombinant apoenzyme in complex with inhibitors N-(3,3-diphenyl-propyl)-nicotinamide and 4-cyano-N-[3-(4-fluorophenyl)-3-(4-methanesulfonyl-phenyl)-propyl]-benzamide, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 12 mg/ml protein in 100 mM sodium phosphate pH 7.4, 50 mM NaCl and 3 mM DTT, is mixed with 0.005 ml of reservoir solution containing 0.2 M lithium sulfate, 36% PEG 3350, and 0.1 M Tris pH 8.4, and 500 nl of 0.006 mM beta-D-hexadecyl maltoside, 4°C, 1 week, X-ray diffraction structure determination and analysis at 1.95-2.5 A resolution
purified recombinant enzyme as apo-crystals of sEH by sitting drop vapor diffusion method, mixing of 15-20 mg/ml protein with reservoir solution containing 0.1 M potassium phosphate, pH 7.5, 0.2 M ammonium dihydrogen phosphate, and 22% w/v PEG 3350, 3-4 days, for inhibitor complexed crystals, soaking in 10 mM ligand in mother liquor for 4 h at room temperature, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement method using PDB ID 1S8O as a search model
purified recombinant enzyme in complex with inhibitors 4-(3-cyclohexylureido)-ethanoic acid, N-cyclohexyl-N'-iodophenyl urea, 4-(3-cyclohexylureido)-butyric acid, 4-(3-cyclohexylureido)-hexanoic acid, and 4-(3-cyclohexylureido)-heptanoic acid, vapour diffusion method, 0.005 ml sitting drops of protein solution containing 12-16 mg/ml enzyme, 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, mixed with 0.005 ml precipitant solution containing 0.1 M Tris, pH 8.4, and 34% w/v PEG3350, and 0.005 ml n-hexadecyl-beta-D-maltoside solution, versus 1 ml reservoir solution, 4°C, 7 days, soaking of crystals in precipitation solution containing 30 mM inhibitor, 3 days, 4°C, cryoprotection by 20% sucrose, X-ray diffraction structure determination and analysis at 2.3-3.0 A resolution
purified recombinant enzyme in complex with N-cyclohexyl-N'-(iodophenyl)urea, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitation solution, 4°C, 10 days, soaking of crystals in inhibitor solution and n-hexadecyl-beta-D-maltoside, X-ray diffraction structure determination and analysis at 2.35 A resolution, modeling
sitting drop vapour diffusion method, X-ray crystal structure determined at 2.6 A resolution, structure of the complex with the inhibitor N-cyclohexyl-N‘-(iodophenyl)urea determine at 2.35 A resolution
using 0.1 M potassium phosphate, pH 7.5, 0.2 M ammonium dihydrogen phosphate, and 22% (w/v) polyethylene glycol PEG3350
wild-type and mutants Y381F, Y465F, Y381F/Y465F. The two active site tyrosine residues act in concert to lower the activation barrier for the alkylation step
analysis of several crystal structures of apoenzyme and enzyme bound to inhibitor urea for molecular dynamics simulations and determination of active site conformation replacing the inhibitor by substrate trans-methylstyrene oxide in the crystal structure model, minimized structure models
enzyme with bound inhibitor N-cyclohexyl-N'-decylurea
-
hanging drop vapor diffusion method, using 30% (w/v) PEG 3350, 0-10% (w/v) sucrose, at 4°C
-