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Literature summary for 3.3.2.10 extracted from

  • Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.
    The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity (2003), Proc. Natl. Acad. Sci. USA, 100, 1558-1563.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in insect cells using the baculovirus infection system Homo sapiens

Protein Variants

Protein Variants Comment Organism
Y465F site-directed mutagenesis, mutant enzyme shows phosphatase, but no epoxide hydrolase activity Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
1,3-dicyclohexyl urea 0.1 mM, complete inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity; complete inhibition at 0.1 mM Homo sapiens
1-cyclohexyl-3-dodecyl urea 0.1 mM, complete inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity; complete inhibition at 0.1 mM Homo sapiens
1-cyclohexyl-3-ethyl urea 0.1 mM, 54% inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity; 54% inhibition at 0.1 mM Homo sapiens
1-cyclohexyl-3-hexyl urea 0.1 mM, complete inhibition of epoxide hydrolase activity, 4% inhibition of phosphatase activity; complete inhibition at 0.1 mM Homo sapiens
4-fluoro-chalcone oxide 0.1 mM, 87% inhibition of epoxide hydrolase activity, 8% inhibition of phosphatase activity Homo sapiens
4-fluorochalcone oxide 87% inhibition at 0.1 mM, competitive substrate Homo sapiens
4-phenyl-chalcone oxide 0.1 mM, complete inhibition of epoxide hydrolase activity, 11% inhibition of phosphatase activity Homo sapiens
4-Phenylchalcone oxide complete inhibition at 0.1 mM, competitive substrate Homo sapiens
Ca2+ inhibition of Mg2+-dependent acrtivity Homo sapiens
Cd2+ inhibition of phosphatase activity and epoxide hydrolase activity Homo sapiens
Ce3+ inhibition of Mg2+-dependent acrtivity Homo sapiens
Chalcone oxide 0.1 mM, 80% inhibition of epoxide hydrolase activity, no inhibition of phosphatase activity; 80% inhibition at 0.1 mM, competitive substrate Homo sapiens
Co2+ inhibition of Mg2+-dependent acrtivity Homo sapiens
Cu+ inhibition of phosphatase activity and epoxide hydrolase activity Homo sapiens
Cu2+ inhibition of phosphatase activity and epoxide hydrolase activity Homo sapiens
Fe2+ inhibition of Mg2+-dependent acrtivity Homo sapiens
Fe3+ inhibition of Mg2+-dependent acrtivity Homo sapiens
Hg2+ inhibition of phosphatase activity and epoxide hydrolase activity Homo sapiens
Mn2+ inhibition of Mg2+-dependent acrtivity Homo sapiens
additional information poor or no inhibition by tartaric acid, sodium fluoride, and sodium molybdate Homo sapiens
okadaic acid 12% inhibition at 0.1 mM Homo sapiens
Pb2+ inhibition of Mg2+-dependent acrtivity Homo sapiens
sodium orthovanadate 9% inhibition at 0.1 mM Homo sapiens
Zn2+ inhibition of phosphatase activity and epoxide hydrolase activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0209
-
threo-10-hydroxy-9-phosphonooxy-octadecanoic acid
-
Homo sapiens
1.6
-
p-nitrophenyl phosphate
-
Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ce3+ enhances activity Homo sapiens
Co2+ 50% of the activation with Mg2+ Homo sapiens
Mg2+ enhances activity Homo sapiens
Ni2+ enhances activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens
-
gene EPXH2
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens
recombinant wild-type and mutant enzymes from insect cells by affinity chromatography Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
an epoxide + H2O = a glycol the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0064
-
epoxide hydrolysis Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
12-phosphonooxyoctadec-9E-enoic acid + H2O
-
Homo sapiens (9E)-octadecenoic acid + phosphate
-
?
12-phosphonooxyoctadec-9Z-enoic acid + H2O
-
Homo sapiens (9Z)-octadecenoic acid + phosphate
-
?
12-phosphonooxyoctadecanoic acid + H2O
-
Homo sapiens octadecanoic acid + phosphate
-
?
erythro-10-hydroxy-9-phosphonooxy-octadecanoic acid + H2O
-
Homo sapiens 10-hydroxy-octadecanoic acid + phosphate
-
?
additional information the N-terminal domain of the enzyme is a functional phosphatase unaffected by a number of classic phosphatase inhibitors. The phosphatase domain has high specificity for lipophilic phosphates Homo sapiens ?
-
?
p-nitrophenyl phosphate + H2O
-
Homo sapiens ?
-
?
threo-10-hydroxy-9-phosphonooxy-octadecanoic acid + H2O
-
Homo sapiens 10-hydroxy-octadecanoic acid + phosphate
-
?
trans-diphenyl propene oxide + H2O
-
Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, structure analysis Homo sapiens

Synonyms

Synonyms Comment Organism
EPXH2
-
Homo sapiens
More see also EC 3.1.3.76 Homo sapiens
SEH
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.06
-
p-nitrophenyl phosphate
-
Homo sapiens
0.35
-
threo-10-hydroxy-9-phosphonooxy-octadecanoic acid
-
Homo sapiens