CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.390 | Neutral Protease; domain 2 |
|
1.10.390.10 | Neutral Protease Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Neutral Protease Domain 2 |
| Functional Family | Leukotriene A(4) hydrolase |
Enzyme Information
| 3.3.2.10 |
Soluble epoxide hydrolase.
based on mapping to UniProt Q10740
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.
|
| 3.4.11.- |
Aminopeptidases.
based on mapping to UniProt Q10740
|
UniProtKB Entries (1)
| Q10740 |
LKHA4_YEAST
Saccharomyces cerevisiae S288C
Leucine aminopeptidase 2
|
PDB Structure
| PDB | 2XPY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A Leukotriene A(4) Hydrolase-Related Aminopeptidase from Yeast Undergoes Induced Fit Upon Inhibitor Binding.
J.Mol.Biol.
|
