X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity
2006 (English)In: Protein Science, ISSN 0961-8368, Vol. 15, no 7, 1628-1637 p.Article in journal (Refereed) Published
Abstract: 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 angstrom. 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.
Place, publisher, year, edition, pages
2006. Vol. 15, no 7, 1628-1637 p.
X-ray crystallography, epoxide hydrolase, active site, trans-stilbene oxide, substrate specificity
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
IdentifiersURN: urn:nbn:se:uu:diva-93349DOI: 10.1110/ps.051792106ISI: 000238707200006OAI: oai:DiVA.org:uu-93349DiVA: diva2:166802