Cytochrome P450-dependent enzyme involved in steroidogenesis (CYP (or specific isoforms such as CYP11A1, CYP17A1, etc., depending on context))

Cytochrome P450-dependent enzymes involved in steroidogenesis are a subset of the large cytochrome P450 superfamily—heme-containing monooxygenases that catalyze key oxidative reactions in the biosynthesis of all major classes of steroid hormones. These reactions include hydroxylation and cleavage steps required for converting cholesterol into pregnenolone and subsequently into glucocorticoids, mineralocorticoids, estrogens, androgens. The active site contains a heme iron center coordinated by a cysteine residue; substrate binding induces conformational changes facilitating electron transfer from NAD(P)H via associated reductases. These enzymes play essential roles not only in normal physiology but also contribute to disease states when dysregulated or mutated—most notably certain cancers where altered steroidogenesis drives tumor growth[1][2][4]. Drugs targeting these proteins are clinically important for managing hormone-dependent diseases but require careful monitoring due to their central role in endocrine homeostasis.

Other names

Cytochrome P450 enzymeSteroidogenic cytochrome P450Steroidogenic CYPHeme-thiolate monooxygenase (steroidogenic)Steroid hydroxylase (for some bacterial homologs)

Drugs targeting these enzymes typically act by inhibiting the heme iron center or blocking substrate access to the active site, thereby reducing or altering the synthesis of downstream steroid hormones. For example, abiraterone inhibits androgen production by blocking CYP17A1 activity.