Evidence map›Paper›PMID 39080270›Full record

ArticleNature communications2024

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

Shengrong Cui, Shumeng Zhang, Ning Wang, Xiaodong Su, Zuliang Luo, Xiaojun Ma, Mei Li

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
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  4. Review
  5. Review
  6. A review ofChinese herbal medicines · 2026
    Review
  7. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Shengrong Cui *Institute of Medicinal Plant Development, Chinese Academy of Medical Sciences and Peking Union Medical College, 100193, Beijing, PR China.ORCID 0000-0002-0704-5610
Shumeng Zhang *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, PR China.ORCID 0000-0002-4617-9224
Ning WangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, PR China.
Xiaodong SuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, PR China.
Zuliang LuoInstitute of Medicinal Plant Development, Chinese Academy of Medical Sciences and Peking Union Medical College, 100193, Beijing, PR China. zuliangluo@163.com.ORCID 0000-0002-7548-341X
Xiaojun MaInstitute of Medicinal Plant Development, Chinese Academy of Medical Sciences and Peking Union Medical College, 100193, Beijing, PR China. mayixuan10@163.com.ORCID 0000-0003-0394-2282
Mei LiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, PR China. meili@ibp.ac.cn.ORCID 0000-0002-1742-2360

Funding

Chinese Academy of Sciences (CAS) XDB37020101Chinese Academy of Sciences (CAS) Y2022038Chinese Academy of Sciences (CAS) YSBR-015National Natural Science Foundation of China (National Science Foundation of China) U20A2004
6 · The paper itself

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.

Indexed as

Catalytic DomainGlycosyltransferasesCatalysisCucurbitaceaeGlycosylationPlant ProteinsSubstrate SpecificitySweetening AgentsTriterpenesGlycosyltransferasesmogroside VPlant ProteinsSweetening AgentsTriterpenes

Identifiers

PMID39080270
PMCPMC11289153

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.