This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2cjp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cjp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2cjp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cjp| PDB=2cjp | SCENE= }}
{{STRUCTURE_2cjp| PDB=2cjp | SCENE= }}
-
'''STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16751602}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16751602 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16751602}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Widersten, M.]]
[[Category: Widersten, M.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:18:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:53:12 2008''

Revision as of 04:53, 29 July 2008

Image:2cjp.png

Template:STRUCTURE 2cjp

STRUCTURE OF POTATO (SOLANUM TUBEROSUM) EPOXIDE HYDROLASE I (STEH1)

Template:ABSTRACT PUBMED 16751602

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 Tue Jul 29 07:53:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cjp"
Personal tools