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Literature summary extracted from

  • Schiott, B.; Bruice, T.C.
    Reaction mechanism of soluble epoxide hydrolase: insights from molecular dynamics simulations (2002), J. Am. Chem. Soc., 124, 14558-14570.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.3.2.10 analysis of several crystal structures of apoenzyme and enzyme bound to inhibitor urea for molecular dynamics simulations and determination of active site conformation replacing the inhibitor by substrate trans-methylstyrene oxide in the crystal structure model, minimized structure models Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.10 Urea
-
 Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.3.2.10 cytosol
-
 Mus musculus 5829
-

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.10 Mus musculus P34914
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.10 an epoxide + H2O = a glycol detailed reaction mechanism, molecular dynamics simulations, detailed analysis of substrate binding to the active site and determination of the preferred conformation, involving Tyr381, Tyr465, and His523 Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.10 (1S,2S)-trans-methylstyrene oxide + H2O a hydrogen bond from Tyr465 to the substrate oxygen is essential for controlling the regioselectivity of the reaction Mus musculus ?
-
 r

Subunits

EC Number Subunits Comment Organism
3.3.2.10 More structure determination and analysis Mus musculus

Synonyms

EC Number Synonyms Comment Organism
3.3.2.10 SEH
-
 Mus musculus