CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.450 | Nuclear Transport Factor 2; Chain: A, |
|
3.10.450.50 |
Domain Context
CATH Clusters
| Superfamily | 3.10.450.50 |
| Functional Family | Epoxide hydrolase EphG |
Enzyme Information
| 3.3.2.10 |
Soluble epoxide hydrolase.
based on mapping to UniProt O33283
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.
|
| 3.3.2.11 |
Cholesterol-5,6-oxide hydrolase.
based on mapping to UniProt O33283
(1) 5,6-alpha-epoxy-5-alpha-cholestan-3-beta-ol + H(2)O = cholestane-3- beta,5-alpha,6-beta-triol. (2) 5,6-beta-epoxy-5-beta-cholestan-3-beta-ol + H(2)O = cholestane-3- beta,5-alpha,6-beta-triol.
-!- The enzyme appears to work equally well with both diastereoisomers of cholesterol 5,6-epoxide. -!- The product is a competitive inhibitor of the reaction.
|
UniProtKB Entries (1)
| O33283 |
EPHG_MYCTU
Mycobacterium tuberculosis H37Rv
Epoxide hydrolase EphG
|
PDB Structure
| PDB | 2BNG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of an Atypical Epoxide Hydrolase from Mycobacterium Tuberculosis Gives Insights Into its Function.
J.Mol.Biol.
|