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Literature summary for 3.3.2.10 extracted from

  • Pinot, F.; Grant, D.F.; Beetham, J.K.; Parker, A.G.; Borhan, B.; Landt, S.; Jones, A.D.; Hammock, B.D.
    Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase (1995), J. Biol. Chem., 270, 7968-7974.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
baculovirus expression system Mus musculus

Protein Variants

Protein Variants Comment Organism
D333N 21.5% of the activity of the wild-type enzyme with trans-stilbene oxide Mus musculus
D333S no detectable activity with trans-stilbene oxide Mus musculus
H237N 117.2% of the activity of the wild-type enzyme with trans-stilbene oxide Mus musculus
H263N 52.3% of the activity of the wild-type enzyme with trans-stilbene oxide Mus musculus
H332N 3.3% of the activity of the wild-type enzyme with trans-stilbene oxide Mus musculus
H523Q 0.1% of the activity of the wild-type enzyme with trans-stilbene oxide Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information involvement of the Asp333-His523 pair in the catalytic mechanism Mus musculus ?
-
?
trans-stilbene oxide + H2O
-
Mus musculus ?
-
?