squalene epoxidase

(redirected from Squalene monooxygenase)
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squa·lene e·pox·i·dase

[MIM*602019]
an enzyme that catalyzes the conversion of squalene to squalene 2,3-oxide in the endoplasmic reticulum; a required step in order for cyclization to occur, resulting in the synthesis of the first sterol, lanosterol, in steroidogenesis; uses NADPH.
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Laden and Porter (2001) have shown that resveratrol reduced cholesterol synthesis by inhibiting squalene monooxygenase in vitro, a rate-limiting enzyme in cholesterol biosynthesis.
Resveratrol inhibits human squalene monooxygenase. Nutr.
Additionally, squalene monooxygenase is exclusively upregulated (8 folds) only in HKI1532 (tolerant genotype).
The chemical form of tellurium involved in squalene monooxygenase inhibition is unknown but tellurite (Te(IV), dimethyltellurium dichloride, and dimethyltelluride can inhibit the brain enzyme from rats [47, 67].
Several of the genes that were found by the microarray study to be more highly transcribed in androgen ablation-resistant tumors encoded biosynthetic enzymes involved in the synthesis of cholesterol, including HMG-CoA synthase, squalene synthase, lanosterol synthase, and squalene monooxygenase, the rate-limiting enzyme in sterol synthesis.