Limonene-1,2-epoxide hydrolase

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='5aig' size='340' side='right' caption='Caption for this structure' scene=''>
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10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
== Function ==
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'''Limonene-1,2-epoxide hydrolase''' (LEH)
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'''Limonene-1,2-epoxide hydrolase''' (LEH) is part of the limonene degradation pathway of ''Rhodococcus erythropolis''. LEH hydrolyzes limonene-1,2-epoxide to produce limonene-1,2-diol<ref>PMID:16218628</ref>.
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== Disease ==
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== Relevance ==
== Relevance ==
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LEH plays important physiological role in detoxification of reactive xenobiotics or endogenous metabolites and in the formation of biologically active mediators<ref>PMID:26032250</ref>.
== Structural highlights ==
== Structural highlights ==

Revision as of 08:26, 24 May 2020

Caption for this structure

Drag the structure with the mouse to rotate

3D structures of limonene-1,2-epoxide hydrolase

Updated on 24-May-2020

1nww - ReLEH - Rhodococcus erythropolis
4xbw, 5cf1, 5cf2, 4xbx, 5jpp - ReLEH (mutant)
4xby, 5ck6, 5yqt, 5yng - ReLEH (mutant) + cyclopentene oxide
5gkw - ReLEH (mutant) + cyclopentanediol
4xdv, 4xbt, 5clk, 5jpu - ReLEH (mutant) + cyclohexanediol
1nu3 - ReLEH (mutant) + valpromide
5yao - ReLEH (mutant) + expoxid
4r9k, 4r9l - ReLEH (mutant) + hydroxyhexanamide
5aih, 5aif, 5aii - mlLEH - metagenomic library
5aig - mlLEH + valpromide

References

  1. Hopmann KH, Hallberg BM, Himo F. Catalytic mechanism of limonene epoxide hydrolase, a theoretical study. J Am Chem Soc. 2005 Oct 19;127(41):14339-47. doi: 10.1021/ja050940p. PMID:16218628 doi:http://dx.doi.org/10.1021/ja050940p
  2. Ferrandi EE, Sayer C, Isupov MN, Annovazzi C, Marchesi C, Iacobone G, Peng X, Bonch-Osmolovskaya E, Wohlgemuth R, Littlechild JA, Monti D. Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. FEBS J. 2015 May 29. doi: 10.1111/febs.13328. PMID:26032250 doi:http://dx.doi.org/10.1111/febs.13328

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Alexander Berchansky, Michal Harel

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