IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-50662-w.html
   My bibliography  Save this article

Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides

Author

Listed:
  • Shengrong Cui

    (Chinese Academy of Medical Sciences and Peking Union Medical College
    Chinese Academy of Sciences)

  • Shumeng Zhang

    (Chinese Academy of Sciences)

  • Ning Wang

    (Chinese Academy of Sciences)

  • Xiaodong Su

    (Chinese Academy of Sciences)

  • Zuliang Luo

    (Chinese Academy of Medical Sciences and Peking Union Medical College)

  • Xiaojun Ma

    (Chinese Academy of Medical Sciences and Peking Union Medical College)

  • Mei Li

    (Chinese Academy of Sciences)

Abstract

Mogrosides constitute a series of natural sweeteners extracted from Siraitia grosvenorii fruits. These mogrosides are glucosylated to different degrees, with mogroside V (M5) and siamenoside I (SIA) being two mogrosides with high intensities of sweetness. SgUGT94-289-3 constitutes a uridine diphosphate (UDP)-dependent glycosyltransferase (UGT) responsible for the biosynthesis of M5 and SIA, by continuously catalyzing glucosylation on mogroside IIe (M2E) and on the subsequent intermediate mogroside products. However, the mechanism of its promiscuous substrate recognition and multiple catalytic modes remains unclear. Here, we report multiple complex structures and the enzymatic characterization of the glycosyltransferase SgUGT94-289-3. We show that SgUGT94-289-3 adopts a dual-pocket organization in its active site, which allows the two structurally distinct reactive ends of mogrosides to be presented from different pockets to the active site for glucosylation reaction, thus enabling both substrate promiscuity and catalytic regioselectivity. We further identified a structural motif that is essential to catalytic activity and regioselectivity, and generated SgUGT94-289-3 mutants with greatly improved M5/SIA production from M2E in an in vitro one-pot setup.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50662-w
    DOI: 10.1038/s41467-024-50662-w
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-50662-w
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-50662-w?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. 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.
    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.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    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. 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.
    3. 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.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-50662-w. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.