title: Isolation of a putative hydroxyacyl enzyme intermediate of an epoxide hydrolase.
abstract: A putative covalent, alpha-hydroxyacyl intermediate was isolated by the brief exposure of murine soluble epoxide hydrolase to its substrate. The reaction was reversed by time and blocked by competitive inhibitors. The formation of the intermediate was dependent upon the concentration of the enzyme and was increased by incubation under acidic conditions. The structure of the intermediate was supported by microchemical methods.
authors.affiliation: Department of Entomology, University of California, Davis.
authors.forename: B D
authors.initials: BD
authors.lastname: Hammock
authors.forename: F
authors.initials: F
authors.lastname: Pinot
authors.forename: J K
authors.initials: JK
authors.lastname: Beetham
authors.forename: D F
authors.initials: DF
authors.lastname: Grant
authors.forename: M E
authors.initials: ME
authors.lastname: Arand
authors.forename: F
authors.initials: F
authors.lastname: Oesch
mesh_terms: D000215:Acylation; D000818:Animals; D004851:Epoxide Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D051379:Mice; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D014316:Tritium
chemical_list: D011994:Recombinant Proteins; D014316:Tritium; D004851:Epoxide Hydrolases