2CJP

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

2CJP の概要

• エントリーDOI: 10.2210/pdb2cjp/pdb
• 分子名称: EPOXIDE HYDROLASE, TETRAETHYLENE GLYCOL, 2-PROPYLPENTANAMIDE, ... (5 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: SOLANUM TUBEROSUM (POTATO)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74710.62

構造登録者

Mowbray, S.L.,Elfstrom, L.T.,Ahlgren, K.M.,Andersson, C.E.,Widersten, M. (登録日: 2006-04-05, 公開日: 2006-06-07, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.95 Å)