Isolation of a putative hydroxyacyl enzyme intermediate of an epoxide hydrolase

Biochem Biophys Res Commun. 1994 Feb 15;198(3):850-6. doi: 10.1006/bbrc.1994.1121.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acylation
  • Animals
  • Epoxide Hydrolases / antagonists & inhibitors
  • Epoxide Hydrolases / isolation & purification
  • Epoxide Hydrolases / metabolism*
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Mice
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Tritium


  • Recombinant Proteins
  • Tritium
  • Epoxide Hydrolases