Epoxide hydrolase
From Proteopedia
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== Function == | == 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.<br /> '''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.<br /> '''Limonene-1,2-epoxide hydrolase''' catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol<ref>PMID:12773375</ref> . | + | '''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<ref>PMID:18585390</ref>.<br /> '''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.<br /> '''Limonene-1,2-epoxide hydrolase''' catalyzes the conversion of limonene-1,2-epoxide to limonene-1,2-diol<ref>PMID:12773375</ref> . |
== Disease == | == Disease == | ||
Revision as of 21:16, 19 January 2016
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3D Structures of epoxide hydrolase
Updated on 19-January-2016
References
- ↑ 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
- ↑ 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
- ↑ 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
