2CJP

Structure of potato (Solanum tuberosum) epoxide hydrolase I (StEH1)

Summary for 2CJP

• Entry DOI: 10.2210/pdb2cjp/pdb
• Descriptor: EPOXIDE HYDROLASE, TETRAETHYLENE GLYCOL, 2-PROPYLPENTANAMIDE, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: SOLANUM TUBEROSUM (POTATO)
• Total number of polymer chains: 2
• Total formula weight: 74710.62

Authors

Mowbray, S.L.,Elfstrom, L.T.,Ahlgren, K.M.,Andersson, C.E.,Widersten, M. (deposition date: 2006-04-05, release date: 2006-06-07, Last modification date: 2023-12-13)

Primary citation

Mowbray, S.L.,Elfstrom, L.T.,Ahlgren, K.M.,Andersson, C.E.,Widersten, M.
X-Ray Structure of Potato Epoxide Hydrolase Sheds Light on Substrate Specificity in Plant Enzymes.
Protein Sci., 15:1628-, 2006

PubMed 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 A. 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.

PubMed: 16751602
DOI: 10.1110/PS.051792106

Experimental method

X-RAY DIFFRACTION (1.95 Å)