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Literature summary for 3.3.2.10 extracted from

  • Arand, M.; Wagner, H.; Oesch, F.
    Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase (1996), J. Biol. Chem., 271, 4223-4229.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D333G no activity Rattus norvegicus
H332Q strong decrease in enzymatic activity due to a change in substrate affinity, Km deviates only slightly from that of the wild-type enzyme, Vmax is reduced to 5% of the wild-type enzyme Rattus norvegicus
H517Y/C521Y no activity Rattus norvegicus
H523D no activity Rattus norvegicus
W334F 7fold increase in Km-value, 2fold enhanced Vmax Rattus norvegicus
W540L no activity Rattus norvegicus
W540L strong decrease in enzymatic activity due to a change in substrate affinity, Km deviates only slightly from that of the wild-type enzyme Rattus norvegicus
W540S no activity Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
4-fluorochalcone oxide
-
Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.006
-
trans-stilbene oxide mutant enzyme W540L Rattus norvegicus
0.007
-
trans-stilbene oxide native enzyme Rattus norvegicus
0.008
-
trans-stilbene oxide recombinant fusion protein expressed in E. coli Rattus norvegicus
0.0085
-
trans-stilbene oxide mutant enzyme H332Q Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Asp333, Asp495 and His523 form the catalytic triad Rattus norvegicus ?
-
?
trans-stilbene oxide + H2O
-
Rattus norvegicus ?
-
?