2cjp

From Proteopedia

Revision as of 15:05, 30 October 2007

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 ... [(full description)]

About this Structure

2CJP is a [Single protein] structure of sequence from [Solanum tuberosum] with PG4, VPR and EDO as [ligands]. Active as [Transferred entry: 3.3.2.9], with EC number [3.3.2.3]. Structure known Active Site: AC1. 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

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