Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase

B. D. Hammock, F. Pinot, J. K. Beetham, D. F. Grant, M. E. Arand, F. Oesch

Research output: Contribution to journalArticle

53 Scopus citations

Abstract

A putative covalent, α-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.

Original languageEnglish (US)
Pages (from-to)850-856
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume198
Issue number3
DOIs
StatePublished - Feb 14 1994

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

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    Hammock, B. D., Pinot, F., Beetham, J. K., Grant, D. F., Arand, M. E., & Oesch, F. (1994). Isolation of a Putative Hydroxyacyl Enzyme Intermediate of an Epoxide Hydrolase. Biochemical and Biophysical Research Communications, 198(3), 850-856. https://doi.org/10.1006/bbrc.1994.1121