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Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides

Author

Listed:
  • Jinzhu Zhang

    (West China Hospital of Sichuan University, Sichuan University)

  • Minghai Tang

    (West China Hospital of Sichuan University, Sichuan University)

  • Yujie Chen

    (West China Hospital of Sichuan University, Sichuan University)

  • Dan Ke

    (West China Hospital of Sichuan University, Sichuan University)

  • Jie Zhou

    (West China Hospital of Sichuan University, Sichuan University)

  • Xinyu Xu

    (West China Hospital of Sichuan University, Sichuan University)

  • Wenxian Yang

    (West China Hospital of Sichuan University, Sichuan University)

  • Jianxiong He

    (West China Hospital of Sichuan University, Sichuan University)

  • Haohao Dong

    (West China Hospital of Sichuan University, Sichuan University)

  • Yuquan Wei

    (West China Hospital of Sichuan University, Sichuan University)

  • James H. Naismith

    (West China Hospital of Sichuan University, Sichuan University
    Wellcome Trust Centre of Human Genomics, Roosevelt Drive
    Rosalind Franklin Institute)

  • Yi Lin

    (Shanghai Jiao Tong University)

  • Xiaofeng Zhu

    (West China Hospital of Sichuan University, Sichuan University)

  • Wei Cheng

    (West China Hospital of Sichuan University, Sichuan University)

Abstract

Steviol glycosides are the intensely sweet components of extracts from Stevia rebaudiana. These molecules comprise an invariant steviol aglycone decorated with variable glycans and could widely serve as a low-calorie sweetener. However, the most desirable steviol glycosides Reb D and Reb M, devoid of unpleasant aftertaste, are naturally produced only in trace amounts due to low levels of specific β (1–2) glucosylation in Stevia. Here, we report the biochemical and structural characterization of OsUGT91C1, a glycosyltransferase from Oryza sativa, which is efficient at catalyzing β (1–2) glucosylation. The enzyme’s ability to bind steviol glycoside substrate in three modes underlies its flexibility to catalyze β (1–2) glucosylation in two distinct orientations as well as β (1–6) glucosylation. Guided by the structural insights, we engineer this enzyme to enhance the desirable β (1–2) glucosylation, eliminate β (1–6) glucosylation, and obtain a promising catalyst for the industrial production of naturally rare but palatable steviol glycosides.

Suggested Citation

  • Jinzhu Zhang & Minghai Tang & Yujie Chen & Dan Ke & Jie Zhou & Xinyu Xu & Wenxian Yang & Jianxiong He & Haohao Dong & Yuquan Wei & James H. Naismith & Yi Lin & Xiaofeng Zhu & Wei Cheng, 2021. "Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27144-4
    DOI: 10.1038/s41467-021-27144-4
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    References listed on IDEAS

    as
    1. Pavol Skubák & Navraj S. Pannu, 2013. "Automatic protein structure solution from weak X-ray data," Nature Communications, Nature, vol. 4(1), pages 1-6, December.
    2. Ting Yang & Jinzhu Zhang & Dan Ke & Wenxian Yang & Minghai Tang & Jian Jiang & Guo Cheng & Jianshu Li & Wei Cheng & Yuquan Wei & Qintong Li & James H. Naismith & Xiaofeng Zhu, 2019. "Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    3. Di Wu & Di Hu & Hao Chen & Guoming Shi & Irfete S. Fetahu & Feizhen Wu & Kimberlie Rabidou & Rui Fang & Li Tan & Shuyun Xu & Hang Liu & Christian Argueta & Lei Zhang & Fei Mao & Guoquan Yan & Jiajia C, 2018. "Glucose-regulated phosphorylation of TET2 by AMPK reveals a pathway linking diabetes to cancer," Nature, Nature, vol. 559(7715), pages 637-641, July.
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    Cited by:

    1. Yameng Xu & Xinglong Wang & Chenyang Zhang & Xuan Zhou & Xianhao Xu & Luyao Han & Xueqin Lv & Yanfeng Liu & Song Liu & Jianghua Li & Guocheng Du & Jian Chen & Rodrigo Ledesma-Amaro & Long Liu, 2022. "De novo biosynthesis of rubusoside and rebaudiosides in engineered yeasts," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Shengrong Cui & Shumeng Zhang & Ning Wang & Xiaodong Su & Zuliang Luo & Xiaojun Ma & Mei Li, 2024. "Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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