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Squalene monooxygenase (or squalene epoxidase) is an enzyme that uses NADPH and molecular oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway.[1] In humans, squalene epoxidase is encoded by the SQLE gene.[2]
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Inhibitors of squalene epoxidase have found application mainly as antifungal drugs:[3]
Since squalene epoxidase is on the biosynthetic pathway leading to cholesterol, inhibitors of this enzyme may also find application in treatment of hypercholesterolemia.[5]
squalene epoxidase is localized to both the endoplasmic reticulum and lipid droplets. Only the ER localized protein is active.
Squalene epoxidase also catalyzes the formation of 2,3;22,23-diepoxysqualene (DOS). DOS is converted to 24(S),25-epoxylanosterol by lanosterol synthase.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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  | Squalene epoxidase as hypocholesterolemic drug target revisited - ScienceDirect - Progress in Lipid Research : Squalene epoxidase as hypocholesterolemic drug target revisited |
| | Characterization of squalene epoxidase activity from the dermatophyte Trichophyton rubrum and its inhibition by terbinafine and other antimycotic agents - Characterization of squalene epoxidase activity from the dermatophyte Trichophyton rubrum and its inhibition by terbinafine and other antimycotic agents -- Favre and Ryder 40 (2): 443 -- Antimicrobial Agents and Chemotherapy |
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