Squalene epoxidase is a flavin-dependent enzyme that converts squalene to 2,3-epoxysqualene during sterol synthesis. The reaction introduces an oxygen-containing epoxide group before later cyclization steps construct the sterol ring system. In the human enzyme, FAD supports oxidation using molecular oxygen and reducing equivalents supplied through a reductase. [ref]
This step illustrates that biosynthetic pathways control both carbon skeletons and oxidation state. Adding a double-bond oxygen functionality and subsequently forming rings are different chemical operations performed by different enzymes. An assay of pathway output cannot locate an inhibition point without measurements of intermediates or a direct enzyme assay.
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