Limonene-1,2-epoxide hydrolase

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Limonene-1,2-epoxide hydrolase catalytic domain
PDB 1nww EBI.jpg
limonene-1,2-epoxide hydrolase
Symbol LEH
Pfam PF07858
Pfam clan CL0051
InterPro IPR013100
SCOP 1nww
OPM superfamily 133
OPM protein 2bng
limonene-1,2-epoxide hydrolase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a limonene-1,2-epoxide hydrolase (EC is an enzyme that catalyzes the chemical reaction

limonene-1,2-epoxide + H2O limonene-1,2-diol

Thus, the two substrates of this enzyme are limonene-1,2-epoxide and H2O, whereas its product is limonene-1,2-diol.

This enzyme belongs to the family of hydrolases, specifically those acting on ether bonds (ether hydrolases). The systematic name of this enzyme class is limonene-1,2-epoxide hydrolase. This enzyme is also called limonene oxide hydrolase. This enzyme participates in limonene and pinene degradation.

Epoxide hydrolases catalyse the hydrolysis of epoxides to corresponding diols, which is important in detoxification, synthesis of signal molecules, or metabolism. Limonene-1,2- epoxide hydrolase (LEH) differs from many other epoxide hydrolases in its structure and its novel one-step catalytic mechanism. Its main fold consists of a six-stranded mixed beta-sheet, with three N-terminal alpha helices packed to one side to create a pocket that extends into the protein core. A fourth helix lies in such a way that it acts as a rim to this pocket. Although mainly lined by hydrophobic residues, this pocket features a cluster of polar groups that lie at its deepest point and constitute the enzymes active site.[1]


  1. ^ Arand M, Hallberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ, de Bont JA, Jones TA, Mowbray SL (June 2003). "Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site". EMBO J. 22 (11): 2583–92. doi:10.1093/emboj/cdg275. PMC 156771Freely accessible. PMID 12773375. 

Further reading[edit]

This article incorporates text from the public domain Pfam and InterPro: IPR013100