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 | RNA polymerase sigma factor |
Enzyme Information
3.3.2.8 |
Limonene-1,2-epoxide hydrolase.
based on mapping to UniProt O33283
1,2-epoxymenth-8-ene + H(2)O = menth-8-ene-1,2-diol.
-!- Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. -!- The enzyme hydrolyzes several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. -!- It differs from the previously described epoxide hydrolases (EC 3.3.2.4, EC 3.3.2.6, EC 3.3.2.7, EC 3.3.2.9 and EC 3.3.2.10) as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.
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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.
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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.
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UniProtKB Entries (1)
O33283 |
EPHG_MYCTU
Mycobacterium tuberculosis H37Rv
Epoxide hydrolase EphG
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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.
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