Epoxide hydrolase

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	== Structural highlights ==		== Structural highlights ==
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Revision as of 13:37, 10 February 2016

spinqualitylabelsall models Human soluble epoxide hydrolase complex with imidazole derivative inhibitor (PDB code 5alf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Epoxide hydrolase (EH) converts epoxides to trans-dihydrodiols which are excreted from the body. Thus, EH acts as a detoxification agent. Epoxides are formed from degradation of aromatic compounds[1]. Bifunctional EH 2 or soluble EH (SEH) is a bifunctional enzyme with the C-terminal domain having EH activity and the N-terminal domain having lipid phosphatase activity. Limonene-1,2-epoxide hydrolase catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol[2] . Disease Inhibitors of Mycobacterium tuberculosis EH such as urea derivatives, are used as anti-tuberculosis drugs. The valpromide inhibitor of EH is used as anti-epileptic drug. Soluble EH plays a role in several diseases including cardiovascular ones and is a drug target for their therapy [3]. Relevance Structural highlights .

3D Structures of epoxide hydrolase

Updated on 10-February-2016

References

1. ↑ Biswal BK, Morisseau C, Garen G, Cherney MM, Garen C, Niu C, Hammock BD, James MN. The molecular structure of epoxide hydrolase B from Mycobacterium tuberculosis and its complex with a urea-based inhibitor. J Mol Biol. 2008 Sep 12;381(4):897-912. Epub 2008 Jun 17. PMID:18585390 doi:10.1016/j.jmb.2008.06.030
2. ↑ Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL. Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J. 2003 Jun 2;22(11):2583-92. PMID:12773375 doi:http://dx.doi.org/10.1093/emboj/cdg275
3. ↑ Imig JD, Hammock BD. Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases. Nat Rev Drug Discov. 2009 Oct;8(10):794-805. doi: 10.1038/nrd2875. PMID:19794443 doi:http://dx.doi.org/10.1038/nrd2875