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X-ray structure of ...
X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity
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- Mowbray, Sherry L. (author)
- Swedish University of Agricultural Sciences, Department of Molecular Biology
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- Elfström, Lisa (author)
- Uppsala universitet,Institutionen för biokemi och organisk kemi
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- Ahlgren, Kerstin (author)
- Uppsala universitet,Institutionen för medicinska vetenskaper
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- Andersson, Evalena (author)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
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- Widersten, Mikael (author)
- Uppsala universitet,Institutionen för biokemi och organisk kemi
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(creator_code:org_t)
- Wiley, 2006
- 2006
- English.
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In: Protein Science. - : Wiley. - 0961-8368 .- 1469-896X. ; 15:7, s. 1628-1637
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Keyword
- X-ray crystallography
- epoxide hydrolase
- active site
- trans-stilbene oxide
- substrate specificity
- Biochemistry
- Biokemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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