Evidence map›Paper›PMID 39888435›Full record

ArticlePlanta2025

Functional characterization and site-directed mutagenesis of a novel UDP-glycosyltransferase from Panax japonicus var. major.

Lu Mou, Yang Zhang, Yu-Xin Zhuang, Rui-Fang Ren, Ran Xu, Ling Yang, Shao-Peng Zhang, Deng-Xiang Du

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Functional Study ofPlants (Basel, Switzerland) · 2025
    Article
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

8 authors.

Lu Mou *National R&D Center for Se-Rich Agricultural Products Processing, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.
Yang Zhang *National R&D Center for Se-Rich Agricultural Products Processing, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.
Yu-Xin ZhuangNational R&D Center for Se-Rich Agricultural Products Processing, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.
Rui-Fang RenNational R&D Center for Se-Rich Agricultural Products Processing, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.
Ran XuSchool of Life Science and Technology, Wuhan Polytechnic University, Wuhan, 430023, China.
Ling YangCollege of Forestry, Beijing Forestry University, Beijing, 100091, China.
Shao-Peng ZhangNational R&D Center for Se-Rich Agricultural Products Processing, School of Modern Industry for Selenium Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China. shaopeng@whpu.edu.cn.ORCID http://orcid.org/0000-0001-9330-0579
Deng-Xiang DuSchool of Life Science and Technology, Wuhan Polytechnic University, Wuhan, 430023, China. ddx@whpu.edu.cn.

Funding

the key project at central government level: the ability establishment of sustainable use for valuable Chinese medicine resources 2060302
6 · The paper itself

Abstract

Ginsenosides R2 and F2 are key active components of Panax japonicus var. major which exhibit a wide range of pharmacological effects. However, few UDP-glycosyltransferases (UGTs) involved in Rh2 and F2 biosynthesis have been identified. In this study, 12 UGTs from Panax japonicus var. major were predicted and characterized. Among them, one UGT (PjvmUGT45) exhibited superior catalytic activities by catalyzing the C3 hydroxyl glycosylation of protopanaxadiol (PPD) and compound K to form Rh2 and F2, respectively. Especially, PjvmUGT45 showed certain substrate specificity and regional specificity at the C-3 sites of PPD-type ginsenosides. Site-directed mutagenesis showed that Gln334, His349, Ser354, and Asp373 were key residues for PjvmUGT45, and the K280A mutant highly improved its activity. Our results revealed the biosynthetic mechanism of ginsenosides in Panax japonicus var. major, providing a novel alternative UGT for ginsenoside Rh2 production by synthetic biological methods.

Indexed as

GinsenosidesGlycosyltransferasesPanaxPlant ProteinsGlycosylationMutagenesis, Site-DirectedSapogeninsSubstrate Specificityginsenoside Rh2GinsenosidesGlycosyltransferasesPlant ProteinsprotopanaxadiolSapogenins

Identifiers

PMID39888435

What OpenQuestion holds

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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.