Enhanced chemoselectivity of a plant cytochrome P450 through protein engineering of surface and catalytic residues.

ABSTRACT: Cytochrome P450s (P450s) are the most versatile catalysts utilized by plants to produce structurally and functionally diverse metabolites. Given the high degree of gene redundancy and challenge to functionally characterize plant P450s, protein engineering is used as a complementary strategy to study the mechanisms of P450-mediated reactions, or to alter their functions. We previously proposed an approach of engineering plant P450s based on combining high-accuracy homology models generated by Rosetta combined with data-driven design using evolutionary information of these enzymes. With this strategy, we repurposed a multi-functional P450 (CYP87D20) into a monooxygenase after redesigning its active site. Since most plant P450s are membrane-anchored proteins that are adapted to the micro-envi

SUBMITTER: Zhang X 

PROVIDER: S-EPMC9590459 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature