CLONING AND EXPRESSION OF SOLUBLE EPOXIDE HYDROLASE FROM POTATO

Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from po tato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to t he carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxi de 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 we re also similar. The expression of sEH in potato was found to be regul ated by both developmental and environmental signals. Levels of mRNA f or sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of ex ogenous methyl jasmonate.