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X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes

¹ Department of Molecular Biology, Swedish University of Agricultural Sciences, SE-751 24 Uppsala, Sweden
² Department of Biochemistry and Organic Chemistry, Uppsala University, SE-751 23 Uppsala, Sweden
³ Department of Cell and Molecular Biology, Uppsala University, SE-751 24 Uppsala, Sweden

(RECEIVED August 18, 2005; FINAL REVISION April 4, 2006; ACCEPTED April 4, 2006)

Epoxide hydrolases catalyze the conversion of epoxides to diols. The known functions of such enzymes include detoxification of xenobiotics, drug metabolism, synthesis of signaling compounds, and intermediary metabolism. In plants, epoxide hydrolases are thought to participate in general defense systems. In the present study, we report the first structure of a plant epoxide hydrolase, one of the four homologous enzymes found in potato. The structure was solved by molecular replacement and refined to a resolution of 1.95 Å. Analysis of the structure allows a better understanding of the observed substrate specificities and activity. Further, comparisons with mammalian and fungal epoxide hydrolase structures reported earlier show the basis of differing substrate specificities in the various epoxide hydrolase subfamilies. Most plant enzymes, like the potato epoxide hydrolase, are expected to be monomers with a preference for substrates with long lipid-like substituents of the epoxide ring. The significance of these results in the context of biological roles and industrial applications is discussed.

Keywords: X-ray crystallography; epoxide hydrolase; active site; trans-stilbene oxide; substrate specificity

Reprint requests to: Sherry Mowbray, Department of Molecular Biology, Swedish University of Agricultural Sciences, Box 590, Biomedical Center, SE-751 24 Uppsala, Sweden; e-mail: mowbray{at}xray.bmc.uu.se; fax: +46-18-53-69-71.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051792106.

Abbreviations: EH, epoxide hydrolase; StEH1, epoxide hydrolase 1 from Solanum tuberosum; ArEH, epoxide hydrolase from Agrobacterium radiobacter AD1; MmsEH, soluble epoxide hydrolase from Mus musculus; HssEH, soluble epoxide hydrolase from Homo sapiens; AnEH, epoxide hydrolase from Aspergillus niger; PEG, polyethylene glycol; RMS, root-mean-square; TSO, trans-stilbene oxide.

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