Cloning and expression of soluble epoxide hydrolase from potato

Andrew Stapleton, Jeffrey K. Beetham, Franck Pinot, Joan E. Garbarino, David R. Rockhold, Mendel Friedman, Bruce D. Hammock, William R. Belknap

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88 Scopus citations

Abstract

Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used diagnostic substrate for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.

Original languageEnglish (US)
Pages (from-to)251-258
Number of pages8
JournalPlant Journal
Volume6
Issue number2
StatePublished - 1994

ASJC Scopus subject areas

  • Plant Science

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    Stapleton, A., Beetham, J. K., Pinot, F., Garbarino, J. E., Rockhold, D. R., Friedman, M., Hammock, B. D., & Belknap, W. R. (1994). Cloning and expression of soluble epoxide hydrolase from potato. Plant Journal, 6(2), 251-258.