Cholesterol-5,6-epoxide hydrolase (ChEH)

Cholesterol-5,6-epoxide hydrolase (ChEH) is an intracellular enzyme primarily localized to the endoplasmic reticulum and, to a lesser extent, the plasma membrane, especially in the liver and other cholesterogenic tissues[3][4]. Its main function is hydrolyzing cholesterol 5,6-epoxides (5,6-ECs), which are oxysterols produced during cholesterol oxidation, into cholestane-3β,5α,6β-triol (CT).[2][4] This conversion regulates the detoxification of potentially genotoxic cholesterol epoxides and is an important checkpoint in cholesterol and oxysterol metabolism[2]. Dysregulation or inhibition of ChEH can lead to the accumulation of toxic intermediates and has been associated with several pathologies, most notably certain cancers and neurodegenerative diseases[2][4]. ChEH is also functionally related to the antiestrogen binding site (AEBS) complex—its pharmacological modulation can affect cell differentiation and apoptosis, notably in tumor cells[4].

Other names

Cholesterol epoxide hydrolaseCholesterol-5,6-oxide hydrolase

Inhibition of ChEH activity (prevents the conversion of cholesterol epoxides to triols, modulating downstream biological effects)