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CATH Superfamily 3.10.450.50

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 21: Epoxide hydrolase EphG

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Cholesterol-5,6-oxide hydrolase. [EC: 3.3.2.11]
(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.
 110 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1
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Soluble epoxide hydrolase. [EC: 3.3.2.10]
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.
 110 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1 A0A045JIR1
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