Engineering a cytochrome P450 enzyme as a peroxygenase for selective hydroxylation of steroids.

ABSTRACT: Selective activation of steroid skeletons is crucial for the generation of pharmaceutically valuable compounds. Despite the success of engineering cytochrome P450 enzymes as peroxygenases to utilize cost-effective H₂O₂, their applications are limited due to poor H₂O₂ tolerance. Here, we report a cytochrome P450 enzyme, namely P450stri, from Streptomyces triculaminicus and its engineering as a peroxygenase with strong H₂O₂ tolerance for regioselective hydroxylation of steroids. We find that a conserved Phe above heme cluster predominantly determines the performance of peroxygenase activity and regioselectivity. Additionally, we reconstruct P450stri by two-dimensional engineering approach based on a Round Flask model to simult

SUBMITTER: Tang T 

PROVIDER: S-EPMC12936177 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature