Cloning and expression of soluble epoxide hydrolase from potato.
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.
Stapleton
A
A
United States Department of Agriculture, Agricultural Research Service, Western Regional Research Center, Albany, CA 94710.
Beetham
J K
JK
Pinot
F
F
Garbarino
J E
JE
Rockhold
D R
DR
Friedman
M
M
Hammock
B D
BD
Belknap
W R
WR
D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers / Q000235:genetics; D018744:DNA, Plant / Q000235:genetics; D004851:Epoxide Hydrolases / Q000235:genetics*; D015870:Gene Expression; D017343:Genes, Plant; D005822:Genetic Vectors; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D011198:Solanum tuberosum / Q000201:enzymology* / Q000235:genetics*; D012995:Solubility; D013045:Species Specificity; D018411:Spodoptera
D017931:DNA Primers; D018744:DNA, Plant; D004851:Epoxide Hydrolases