Function
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[1].
Relevance
LEH plays important physiological role in detoxification of reactive xenobiotics or endogenous metabolites and in the formation of biologically active mediators[2].
Structural highlights
The complex of LEH with the valpromide inhibitor shows the valpromide in the LEH active site forming a hydrogen bond network. Water molecule is shown as red sphere. In the LEH hydrolysis mechanism residue Asp101 acts as the acid and Asp132 as the base [3].
- ↑ 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:https://dx.doi.org/10.1021/ja050940p
- ↑ 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:https://dx.doi.org/10.1093/emboj/cdg275
- ↑ 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:https://dx.doi.org/10.1111/febs.13328
