CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1000 | HAD superfamily/HAD-like |
Domain Context
CATH Clusters
| Superfamily | HAD superfamily/HAD-like |
| 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 | 3I28 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure-based optimization of arylamides as inhibitors of soluble epoxide hydrolase.
J.Med.Chem.
|