CATH Domain 3otqA01

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	3OTQ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Substituted pyrazoles as novel sEH antagonist: investigation of key binding interactions within the catalytic domain. Lo, H.Y., Man, C.C., Fleck, R.W., Farrow, N.A., Ingraham, R.H., Kukulka, A., Proudfoot, J.R., Betageri, R., Kirrane, T., Patel, U., Sharma, R., Hoermann, M.A., Kabcenell, A., Lombaert, S.D. Bioorg.Med.Chem.Lett.