CYP17A1

CYP17A1 is a cytochrome P450 enzyme that drives steroidogenesis by catalyzing 17α-hydroxylation and 17,20-lyase reactions required for androgen precursor formation^[1]. Mechanistically, this dual activity connects pregnenolone and progesterone metabolism with androgen biosynthesis, making CYP17A1 central to steroid hormone research^[1][2]. In disease models, CYP17A1 supports androgen production relevant to castration-resistant prostate cancer, where abiraterone suppresses tumor growth by inhibiting this steroidogenic enzyme^[3]. Compared with teleost Cyp17a2, which shows only 17α-hydroxylase activity, Cyp17a1 retains both 17α-hydroxylase and 17,20-lyase activities, supporting isoform-specific experimental design^[4]. For inhibitor research, abiraterone and TOK-001 structures reveal active-site binding features useful for CYP17A1 drug-design studies, while non-steroidal CYP17A1 inhibitors support selectivity-focused medicinal chemistry^[5][6].