Evidence map›Paper›PMID 39932927›Full record

ArticlePlant biotechnology journal2025

Structure-based virtual screening aids the identification of glycosyltransferases in the biosynthesis of salidroside.

Yan Yao, Fangfang Chen, Chaoyan Wu, Xiaosa Chang, Weijia Cheng, Qiuxia Wang, Zixin Deng, Tiangang Liu, Li Lu

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Article in Plant biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

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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

9 authors.

Yan Yao *Department of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Fangfang Chen *Department of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Chaoyan Wu *Department of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Xiaosa ChangDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Weijia ChengDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Qiuxia WangDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Zixin DengDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Tiangang LiuDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Li LuDepartment of Integrated Traditional Chinese Medicine and Western Medicine, Zhongnan Hospital of Wuhan University, School of Pharmaceutical Sciences, Wuhan University, Wuhan, China.ORCID https://orcid.org/0000-0003-0490-7163

Funding

National Key Research and Development Program of China 2022YFA0912100National Natural Science Foundation of China 32100413
6 · The paper itself

Abstract

Glycosylation plays an important role in the structural diversification of plant natural products. The identification of efficient glycosyltransferases is also a crucial step for the biosynthesis of valuable glycoside products. However, functional characterization of glycosyltransferases (GTs) from an extensive plant gene list is labour-intensive and challenging. Salidroside is a bioactive component derived from plants, widely utilized in the fields of food and medicine. Here, through transcriptome analysis and structure-based virtual screening, we identified two GTs that participated in the biosynthesis of salidroside from a rarely studied herbaceous plant, Astilbe chinensis. Ach15909 was found to possess high catalytic activity as evidenced by the determination of its catalytic parameters. The key residues that determine its catalytic activity were further determined. Additionally, Ach15909 shows a preference for substrates with a volume of <150 Å

Indexed as

GlucosidesGlycosyltransferasesPhenolsPlant ProteinsGlycosylationSubstrate SpecificityGlucosidesGlycosyltransferasesPhenolsPlant Proteinsrhodiolosideglycosyltransferasesinterdomain linkermolecular dockingplant biosynthetic enzymeprotein structure predictionsalidroside

Identifiers

PMID39932927
PMCPMC12018814

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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.