Cloned (Comment) | Organism |
---|---|
expressed in HepG2 cells | Homo sapiens |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Mus musculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Mus musculus | - |
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 | 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 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 |