SummaryA cDNA (1122 bp) was isolated from a cDNA library prepared from Arabidopais thaliana L. that had been subjected to drought stress for I h. The sequencing of a genomic clone corresponding to the cDNA and Sl mepplng analysis revealed that the cDNA lacked the first 6 bp from its translational start (ATG). The resulting open reading frame encodes a polypaptlde of 321 amino acids, and the calculated molecular weight of this polypeptide is 36 423 De. The deduced amino acid sequence shows a high degree of similarity to C terminal halves of those of soluble epoxide hydrolases (sEHs) of human, mouse and rat, 35.5%, 34.1% and 33.1%, respectively. The cDNA was expressed In Escherichla coil cells, and the expressed protein migrates at 40 kDa when analyzed by SDS-PAGE. The recombinant protein at 40 kDa Is much smaller than the mammalian sEH (58 kDa) but has characteristics of activity and inhibition slmller to the mammalian sEHs when assayed with the substrate trans-stilbene oxide and the inhibitors 4-fluorochalcone oxide (4FCO), (2R,3R)-3-(4-nitrophenyl) glycidol (RRNPG), and (2S,3S)-3-(4-nitrophenyl)glycidol (SSNPG), which indicates that the cDNA did encode a soluble epoxide hydrolese of A. thallana (AtsEH). Drought stress, but not heat or cold stress, slightly Increased the accu-