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Squalene monooxygenase

mammalian protein found in Homo sapiens

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionJul 30, 2025
Entity authorityQ414248 ↗
Source-derived summary

Squalene monooxygenase (also called squalene epoxidase) is a eukaryotic enzyme that uses NADPH and diatomic 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. In humans, squalene epoxidase is encoded by the SQLE gene.

Several eukaryote genomes lack a squalene monooxygenase encoding gene, but instead encode an alternative squalene epoxidase that performs the same task.

Mechanism

The canonical squalene monooxygenase is a flavoprotein monooxygenase. Flavoprotein monooxygenase form flavin hydroperoxides at the enzyme active site, which then transfer the terminal oxygen atom of the hydroperoxide to the substrate. Squalene monooxygenase differs from other flavin monooxygenases in that the oxygen is inserted into the substrate as an epoxide rather than as a hydroxyl group. This enzyme contains a loosely bound FAD flavin and obtains electrons from NADPH-cytochrome P450 reductase, rather than binding NADPH directly. The alternative squalene epoxidase belongs to the fatty acid hydroxylase superfamily and obtains electrons from cytochrome b5.

Inhibitors

Inhibitors of squalene epoxidase have found application mainly as antifungal drugs:

butenafine

naftifine

terbinafine

Since squalene epoxidase is on the biosynthetic pathway leading to production of cholesterol, inhibitors of this enzyme may also find application in treatment of hypercholesterolemia.

Editorial summary

This brief starts where responsible research should: with the source description of “Squalene monooxygenase” as mammalian protein found in Homo sapiens. Everything that follows is an evidence route, not borrowed authority.

Editorial reviewA concise reference frame for defining the subject, testing terminology and identifying the institution closest to the evidence. The current 211-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. The account is most persuasive where Squalene, monooxygenase and mammalian can be independently traced.
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The subject matters to the general reference register because the source frames it as mammalian protein found in Homo sapiens. Its deeper value depends on whether names, dates, institutions and citations support that framing.

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Vocabulary and entity names are the principal evidence signals here, because they determine the precision of every later search. The source revision retrieved here is dated Jul 30, 2025. The linked authority identifier is Q414248. None of the 0 selected statements returned an explicit reference.

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This entry incorporates text from “Squalene monooxygenase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.