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Literature summary for 3.3.2.10 extracted from

  • EnayetAllah, A.E.; Luria, A.; Luo, B.; Tsai, H.J.; Sura, P.; Hammock, B.D.; Grant, D.F.
    Opposite regulation of cholesterol levels by the phosphatase and hydrolase domains of soluble epoxide hydrolase (2008), J. Biol. Chem., 283, 36592-36598.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HepG2 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
D335S hydrolase knock-out construct, the mutant enzyme displays only phosphatase activity Mus musculus
D335S hydrolase knock-out construct, the mutant enzyme displays only phosphatase activity Homo sapiens
D9A phosphatase knock-out construct, the mutant enzyme displays only hydrolase activity Mus musculus
D9A phosphatase knock-out construct, the mutant enzyme displays only hydrolase activity Homo sapiens
D9A/D335S sEH protein with mutated phosphatase and hydrolase active sites, the mutant is inactive Mus musculus
D9A/D335S sEH protein with mutated phosphatase and hydrolase active sites, the mutant is inactive Homo sapiens
R287Q the mutant shows lower hydrolase activity than the wild type enzyme Mus musculus
R287Q the mutant shows lower hydrolase activity than the wild type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea potent inhibitor of sEH Homo sapiens
1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea potent inhibitor of sEH Mus musculus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trans-1,3-diphenylpropene oxide + H2O
-
Mus musculus 1,3-diphenylpropane-1,2-diol
-
?
trans-1,3-diphenylpropene oxide + H2O
-
Homo sapiens 1,3-diphenylpropane-1,2-diol
-
?

Synonyms

Synonyms Comment Organism
EC 3.3.2.3
-
Homo sapiens
SEH sEH is a bifunctional enzyme with two catalytic domains: a C-terminal epoxide hydrolase domain and an N-terminal phosphatase domain Mus musculus
SEH sEH is a bifunctional enzyme with two catalytic domains: a C-terminal epoxide hydrolase domain and an N-terminal phosphatase domain Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000003
-
-
Homo sapiens 1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea
0.000005
-
-
Mus musculus 1-(1-methylsulfonyl-piperidin-4-yl)-3-(4-trifluoromethoxy-phenyl)-urea