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Significance We carried out functional analysis of the oat enzyme AsCYP51H10, which is a divergent member of the CYP51 cytochrome P450 family and showed that this enzyme is able to catalyze both hydroxylation and epoxidation of the simple triterpene β-amyrin to give 12,13β-epoxy-3β,16β-dihydroxy-oleanane (12,13β-epoxy-16β-hydroxy-β-amyrin). In contrast, the canonical CYP51 enzymes are highly conserved and catalyze only sterol demethylation. We further show that the C12,13 epoxy group is critical for antifungal activity, a discovery that has important implications for triterpene metabolic engineering for food, health, and industrial biotechnology applications.

Biochemical analysis of a multifunctional cytochrome P450 (CYP51) enzyme required for synthesis of antimicrobial triterpenes in plants