J Integr Plant Biol ›› 2026, Vol. 68 ›› Issue (4): 1218-1230.DOI: 10.1111/jipb.70202

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  • 收稿日期:2025-09-08 接受日期:2026-01-30 出版日期:2026-04-15 发布日期:2026-04-17

Functional characterization of plant UGT93s producing prenylated phenolic glycosides

Hong-Ye Li1†, Jian-Lin Zou1†, Bao Nie2†, Zi-Long Wang1, Meng Zhang1, Chun-Xue Zhao1, Yan-Fang Yang1, Xi-Ran Zhang1, Xin-Yue Zhan2, Li Wang2* and Min Ye1*   

  1. 1. State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China
    2. Shenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Key Laboratory of Synthetic Biology, Ministry of Agriculture and Rural Affairs, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen 518120, China
    †These authors contributed equally to this work.
    *Correspondences: Min Ye (yemin@bjmu.edu.cn, Dr. Ye is fully responsible for the distribution of all materials associated with this article); Li Wang (wangli03@caas.cn)
  • Received:2025-09-08 Accepted:2026-01-30 Online:2026-04-15 Published:2026-04-17
  • Supported by:
    This work was supported by the National Key Research and Development Program of China (No. 2023YFA0914100 to M.Y., and No. 2023YFA0915800 to L.W.), Beijing Natural Science Foundation (No. QY23076 to J.L.Z., and 83001Y0439 to C.X.Z.), National Natural Science Foundation of China (No. 32470245 to L.W., 32400192 to B.N.), Joint Funds of the National Natural Science Foundation of China (No. U24A20358 to B. N.) and Shenzhen Science and Technology Program (No. JCYJ20241202130723030 to L.W.).

Abstract: Prenylated phenolic glycosides, such as nodakenin, represent a class of natural products with diverse bioactivities. Their metabolic engineering production remains largely unexplored, primarily due to the scarcity of efficient UDP-glycosyltransferases (UGTs) capable of catalyzing prenylated phenolic substrates. In this study, we characterized several UGT93 enzymes from Angelica decursiva that catalyzed the glycosylation of nodakenetin. Enzymatic assays revealed a pronounced catalytic preference of these enzymes toward various types of prenylated phenolic substrates. Notably, this substrate preference is conserved across UGT93s from other species and a reconstructed ancestral enzyme. Structural analysis and mutation experiments revealed that the preference was caused by the substrate binding with several hydrophobic and aromatic residues. This study highlights the biocatalytic potential of the UGT93 family enzymes, offering promising biocatalysts for the glycosylation of plant-derived prenylated phenolics.

Key words: Angelica decursiva, biosynthesis, prenylated phenolics, UGT93

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