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Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations

Author

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  • Ting Yang

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

  • Jinzhu Zhang

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

  • Dan Ke

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

  • Wenxian Yang

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

  • Minghai Tang

    (West China Hospital, Sichuan University)

  • Jian Jiang

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

  • Guo Cheng

    (West China School of Public Health, Healthy Food Evaluation Research Center and State Key Laboratory of Biotherapy and Cancer Center, Sichuan University)

  • Jianshu Li

    (College of Polymer Science and Engineering and State Key Laboratory of Polymer Materials Engineering, Sichuan University)

  • Wei Cheng

    (West China Hospital, Sichuan University)

  • Yuquan Wei

    (West China Hospital, Sichuan University)

  • Qintong Li

    (Ministry of Education, Sichuan University)

  • James H. Naismith

    (West China Hospital, Sichuan University
    Division of Structural Biology, Wellcome Trust Centre of Human Genomics
    Rosalind Franklin Institute, Harwell Campus)

  • Xiaofeng Zhu

    (Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University)

Abstract

Diets high in sugar are recognized as a serious health problem, and there is a drive to reduce their consumption. Steviol glycosides are natural zero-calorie sweeteners, but the most desirable ones are biosynthesized with low yields. UGT76G1 catalyzes the β (1–3) addition of glucose to steviol glycosides, which gives them the preferred taste. UGT76G1 is able to transfer glucose to multiple steviol substrates yet remains highly specific in the glycosidic linkage it creates. Here, we report multiple complex structures of the enzyme combined with biochemical data, which reveal that the enzyme utilizes hydrophobic interactions for substrate recognition. The lack of a strict three-dimensional recognition arrangement, typical of hydrogen bonds, permits two different orientations for β (1–3) sugar addition. The use of hydrophobic recognition is unusual in a regio- and stereo-specific catalysis. Harnessing such non-specific hydrophobic interactions could have wide applications in the synthesis of complex glycoconjugates.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11154-4
    DOI: 10.1038/s41467-019-11154-4
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    Cited by:

    1. Shao-Yang Li & Gao-Qian Wang & Liang Long & Jia-Ling Gao & Zheng-Qun Zhou & Yong-Heng Wang & Jian-Ming Lv & Guo-Dong Chen & Dan Hu & Ikuro Abe & Hao Gao, 2024. "Functional and structural dissection of glycosyltransferases underlying the glycodiversity of wolfberry-derived bioactive ingredients lycibarbarspermidines," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. 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.
    3. 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.
    4. 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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