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Published online before print June 2, 2006, 10.1110/ps.051792106
Protein Science (2006), 15:1628-1637. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes

Sherry L. Mowbray1, Lisa T. Elfström2, Kerstin M. Ahlgren1,4, C. Evalena Andersson3 and Mikael Widersten2

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


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A. Thomaeus, A. Naworyta, S. L. Mowbray, and M. Widersten
Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability
Protein Sci., July 1, 2008; 17(7): 1275 - 1284.
[Abstract] [Full Text] [PDF]


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