CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.1820 | alpha/beta hydrolase |
Domain Context
CATH Clusters
Superfamily | alpha/beta hydrolase |
Functional Family | Bifunctional epoxide hydrolase 2 |
Enzyme Information
3.1.3.76 |
Lipid-phosphate phosphatase.
based on mapping to UniProt P34914
(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.
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3.3.2.10 |
Soluble epoxide hydrolase.
based on mapping to UniProt P34914
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.
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UniProtKB Entries (1)
P34914 |
HYES_MOUSE
Mus musculus
Bifunctional epoxide hydrolase 2
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PDB Structure
PDB | 1EK2 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Spodoptera |
Primary Citation |
Binding of alkylurea inhibitors to epoxide hydrolase implicates active site tyrosines in substrate activation.
J.Biol.Chem.
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