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Cloning and expression of soluble epoxide hydrolase from potato
Authors:Andrew Stapleton  Jeffrey K Beetham  Franck Pinot  Joan E Garbarino  David R Rockhold  Mendel Friedman  Bruce D Hammock  William R Belknap
Institution:United States Department of Agriculture, Agricultural Research Service, Western Regional Research Center, 800 Buchanan St., Albany, CA 94710, USA; Department of Biochemistry and Biophysics, and;Department of Entomology and Environmental Toxicology, University of California, Davis, CA 95616, USA
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.
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