CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.10 | Orthogonal Bundle | 
|   | 1.10.150 | DNA polymerase; domain 1 | 
|   | 1.10.150.240 | Putative phosphatase; domain 2 | 
Domain Context
CATH Clusters
| Superfamily | Putative phosphatase; domain 2 | 
| Functional Family | Bifunctional epoxide hydrolase 2 | 
Enzyme Information
| 3.3.2.10 | Soluble epoxide hydrolase. based on mapping to UniProt P34913 An epoxide + H(2)O = a glycol. -!- Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism. -!- It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides. -!- The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76. -!- Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate. -!- The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product. -!- Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64. | 
| 3.1.3.76 | Lipid-phosphate phosphatase. based on mapping to UniProt P34913 (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)- 9,10-dihydroxyoctadecanoate + phosphate. -!- The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10. -!- The best substrates for this enzyme are 10-hydroxy-9- (phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form. -!- The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9. | 
UniProtKB Entries (1)
| P34913 | HYES_HUMAN Homo sapiens Bifunctional epoxide hydrolase 2 | 
PDB Structure
| PDB | 4Y2V | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Identification of N-ethylmethylamine as a novel scaffold for inhibitors of soluble epoxide hydrolase by crystallographic fragment screening Bioorg.Med.Chem. | 
