NMR-guided identification of CYP11A1-Adrenodoxin interactions that differentially govern cholesterol and vitamin D3 metabolism.

ABSTRACT: Cytochromes P450 (CYPs) are heme-containing enzymes essential for a range of biochemical processes, including steroidogenesis and vitamin D metabolism. Among mitochondrial CYPs, CYP11A1 catalyzes both cholesterol side-chain cleavage, producing pregnenolone, and hydroxylation of vitamin D3, producing 20(OH)D3. Previous studies have shown that substrates can modulate CYP11A1 protein-protein interactions with the redox partner Adrenodoxin (Adx), but the structural basis of the substrate-specific modulation towards Adx is not known. In this study, we investigated whether there exist contact(s) between CYP11A1 and Adx that are differentially influenced by cholesterol and vitamin D3, and whether these substrate-specific contacts are important for CYP11A1 monooxygenation of vitamin D3 or side cha

SUBMITTER: McGlohon JE 

PROVIDER: S-EPMC12309602 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature