Gene evolution of epoxide hydrolases and recommended nomenclature

J. K. Beetham, D. Grant, M. Arand, J. Garbarino, T. Kiyosue, F. Pinot, F. Oesch, W. R. Belknap, K. Shinozaki, B. D. Hammock

Research output: Contribution to journalArticlepeer-review

119 Scopus citations


We have analyzed amino acid sequence relationships among soluble and microsomal epoxide hydrolases, haloacid dehalogenases, and a haloalkane dehalogenase. The amino-terminal residues (1-229) of mammalian soluble epoxide hydrolase are homologous to a haloacid dehalogenase. The carboxy- terminal residues (230-554) of mammalian soluble epoxide hydrolase are homologous to haloalkane dehalogenase, to plant soluble epoxide hydrolase, and to microsomal epoxide hydrolase. The shared identity between the haloacid and haloalkane dehalogenases does not indicate relatedness between these two types of dehalogenases. The amino-terminal and carboxy-terminal homologies of mammalian soluble epoxide hydrolase to the respective dehalogenases suggests that this epoxide hydrolase, but not the soluble epoxide hydrolase of plant or the microsomal epoxide hydrolase, derives from a gene fusion. The homology of microsomal to soluble epoxide hydrolase suggests they derive from a gene duplication, probably of an ancestral bacterial (epoxide) hydrolase gene. Based on homology to haloalkane dehalogenase, the catalytic residues for the soluble and microsomal epoxide hydrolases are predicted. A nomenclature system based on divergent molecular evolution is proposed for these epoxide hydrolases.

Original languageEnglish (US)
Pages (from-to)61-71
Number of pages11
JournalDNA and Cell Biology
Issue number1
StatePublished - 1995

ASJC Scopus subject areas

  • Cell Biology
  • Genetics
  • Molecular Biology


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