ArticleThe Biochemical journal2020
Structure-based enzyme engineering improves donor-substrate recognition of Arabidopsis thaliana glycosyltransferases.
Article in The Biochemical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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.
Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- Advances in UDP-Glycosyltransferases from Medicinal Plants: Discovery, Catalytic Mechanism, Engineering and Biosynthetic Application.Metabolites · 2026Review
- Glycosylated cannabinoids inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Article
- Identification and Functional Verification of the Glycosyltransferase Gene Family Involved in Flavonoid Synthesis inPlants (Basel, Switzerland) · 2024Article
- Deciphering the Coevolutionary Dynamics of L2 β-Lactamases via Deep Learning.Journal of chemical information and modeling · 2024Article
- Enzymatic properties of UDP-glycosyltransferase 89B1 from radish and modulation of enzyme catalytic activity via loop region mutation.PloS one · 2024Article
- The sugar donor specificity of plant family 1 glycosyltransferases.Frontiers in bioengineering and biotechnology · 2024Review
- Machine Learning-Guided Protein Engineering.ACS catalysis · 2023Review
- Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.Protein science : a publication of the Protein Society · 2023Article
- Protein Modelling Highlighted Key Catalytic Sites Involved in Position-Specific Glycosylation of Isoflavonoids.International journal of molecular sciences · 2023Article
- Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023Review
- Applications of protein engineering in the microbial synthesis of plant triterpenoids.Synthetic and systems biotechnology · 2023Review
- Gating interactions steer loop conformational changes in the active site of the L1 metallo-β-lactamase.eLife · 2023Article
- Opposite trends of glycosides and alkaloids in Dendrobium nobile of different age based on UPLC-Q/TOF-MS combined with multivariate statistical analyses.Phytochemical analysis : PCA · 2022Article
- Docking-guided rational engineering of a macrolide glycosyltransferase glycodiversifies epothilone B.Communications biology · 2022Article
- Characterization of 5-Plant biotechnology (Tokyo, Japan) · 2021Article
- The Role of Hydrophobic Nodes in the Dynamics of Class A β-Lactamases.Frontiers in microbiology · 2021Article
- Inter-Subunit Dynamics Controls Tunnel Formation During the Oxygenation Process in Hemocyanin Hexamers.Frontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation of secondary metabolites involves plant UDP-dependent glycosyltransferases (UGTs). UGTs have shown promise as catalysts in the synthesis of glycosides for medical treatment. However, limited understanding at the molecular level due to insufficient biochemical and structural information has hindered potential applications of most of these UGTs. In the absence of experimental crystal structures, we employed advanced molecular modeling and simulations in conjunction with biochemical characterization to design a workflow to study five Group H Arabidopsis thaliana (76E1, 76E2, 76E4, 76E5, 76D1) UGTs. Based on our rational structural manipulation and analysis, we identified key amino acids (P129 in 76D1; D374 in 76E2; K275 in 76E4), which when mutated improved donor substrate recognition than wildtype UGTs. Molecular dynamics simulations and deep learning analysis identified structural differences, which drive substrate preferences. The design of these UGTs with broader substrate specificity may play important role in biotechnological and industrial applications. These findings can also serve as basis to study other plant UGTs and thereby advancing UGT enzyme engineering.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.