Identification and Catalytic Optimization of Pinene Oxidases in Paeoniflorin Biosynthetic Pathway

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ID: 328888
2026
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Abstract
Paeoniflorin is a pharmacologically important cage-like monoterpene glycoside characteristic of Paeonia plants, yet its biosynthetic pathway has remained largely unresolved, hindering sustainable production. Here, we confirmed that paeoniflorin biosynthesis originates from α-pinene and identified three novel cytochrome P450 enzymes that catalyze pinene oxidation. CYP71AN126 catalyzes the hydroxylation of α-pinene at positions C4 and C10, followed by further oxidation of the alcohol to a ketone at C4, whereas CYP76A225/226 exclusively catalyze C10 hydroxylation. Virus-induced gene silencing (VIGS) assays demonstrated that silencing CYP71AN126, but not CYP76A225 and CYP76A226, significantly reduced the paeoniflorin content, indicating that C4 hydroxylation plays an important role in paeoniflorin biosynthesis, whereas C10 hydroxylation is not. Through the analysis of natural sequence and activity divergence among CYP71AN126 and CYP76A225/226, combined with protein structure prediction and site-directed mutagenesis, we identified L493 as a critical residue involved in regulating catalytic site specificity and substrate specificity of CYP71AN126. Mutation of L493 reduced or eliminated the formation of undesired C10 hydroxylation side-product and enhanced substrate specificity. These findings establish C4 oxidation of α-pinene as the critical committed step in paeoniflorin biosynthesis. Our study lays a foundation for elucidating the complete biosynthetic pathway of paeoniflorin in Paeonia and provides a target for enzyme engineering of CYP71AN126 aimed at the efficient production of paeoniflorin via synthetic biology approaches.
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Authors Xirui Tan, X.-S. Chen, Longji Wang, Tianlin Pei, Jiewei Zhu, Wenlu Cai, Sanming Zhu, 闫忠荣, Yu Kong, Ying Zhang, Qing Zhao, Xiao‐Ya Chen, Jianxu Li, Shuiyan Yu, Yonghong Hu
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Journal Plant physiology and biochemistry : PPB
Year 2026
DOI
10.1093/plphys/kiag669
URL
https://academic.oup.com/plphys/advance-article-pdf/doi/10.1093/plphys/kiag669/71083235/kiag669.pdf
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