2cjp
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Epoxide hydrolases catalyze the conversion of epoxides to diols. The known | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Solanum tuberosum]] | [[Category: Solanum tuberosum]] | ||
| - | [[Category: Transferred entry: 3 | + | [[Category: Transferred entry: 3 3.2 9]] |
| - | [[Category: Ahlgren, K | + | [[Category: Ahlgren, K M.]] |
| - | [[Category: Andersson, C | + | [[Category: Andersson, C E.]] |
| - | [[Category: Elfstrom, L | + | [[Category: Elfstrom, L T.]] |
| - | [[Category: Mowbray, S | + | [[Category: Mowbray, S L.]] |
[[Category: Widersten, M.]] | [[Category: Widersten, M.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
| Line 24: | Line 24: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:49:22 2008'' |
Revision as of 14:49, 21 February 2008
|
STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)
Overview
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.
About this Structure
2CJP is a Single protein structure of sequence from Solanum tuberosum with , and as ligands. Active as Transferred entry: 3.3.2.9, with EC number 3.3.2.3 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
X-ray structure of potato epoxide hydrolase sheds light on substrate specificity in plant enzymes., Mowbray SL, Elfstrom LT, Ahlgren KM, Andersson CE, Widersten M, Protein Sci. 2006 Jul;15(7):1628-37. Epub 2006 Jun 2. PMID:16751602
Page seeded by OCA on Thu Feb 21 16:49:22 2008
