2cjp

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[[Image:2cjp.gif|left|200px]]
[[Image:2cjp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2cjp |SIZE=350|CAPTION= <scene name='initialview01'>2cjp</scene>, resolution 1.95&Aring;
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The line below this paragraph, containing "STRUCTURE_2cjp", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=VPR:2-PROPYLPENTANAMIDE'>VPR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Microsomal_epoxide_hydrolase Microsomal epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 3.3.2.9] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2cjp| PDB=2cjp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjp OCA], [http://www.ebi.ac.uk/pdbsum/2cjp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cjp RCSB]</span>
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}}
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'''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''
'''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''
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[[Category: Mowbray, S L.]]
[[Category: Mowbray, S L.]]
[[Category: Widersten, M.]]
[[Category: Widersten, M.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:18:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:28 2008''
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Revision as of 19:18, 3 May 2008

Image:2cjp.gif

Template:STRUCTURE 2cjp

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. 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 Sat May 3 22:18:26 2008

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