ArticleMicrobial cell factories2022
Identification of a flavonoid C-glycosyltransferase from fern species Stenoloma chusanum and the application in synthesizing flavonoid C-glycosides in Escherichia coli.
Article in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Sustainable Natural Product Glycosylation: A Critical Evaluation of Biocatalytic and Chemical Approaches.ChemSusChem · 2025Review
- A model for the adaptation of Euryale ferox leaves to aquatic environments through EfCGT1-controlled flavonoid C-glycoside-specific accumulation in epidermis cells.Plant biotechnology journal · 2025Article
- UGT708S6 from Dendrobium catenatum, catalyzes the formation of flavonoid C-glycosides.BMC biotechnology · 2024Article
- Enzymatic Glycosylation of 4'-Hydroxychalcones: Expanding the Scope of Nature's Catalytic Potential.International journal of molecular sciences · 2024Article
- Review
- Glycoside-metabolizing oxidoreductase D3dgpA from human gut bacterium.Frontiers in bioengineering and biotechnology · 2024Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
backgroundFlavonoid C-glycosides have many beneficial effects and are widely used in food and medicine. However, plants contain a limited number of flavonoid C-glycosides, and it is challenging to create these substances chemically.
resultsTo screen more robust C-glycosyltransferases (CGTs) for the biosynthesis of flavonoid C-glycosides, one CGT enzyme from Stenoloma chusanum (ScCGT1) was characterized. Biochemical analyses revealed that ScCGT1 showed the C-glycosylation activity for phloretin, 2-hydroxynaringenin, and 2-hydroxyeriodictyol. Structure modeling and mutagenesis experiments indicated that the glycosylation of ScCGT1 may be initiated by the synergistic action of conserved residue His26 and Asp14. The P164T mutation increased C-glycosylation activity by forming a hydrogen bond with the sugar donor. Furthermore, when using phloretin as a substrate, the extracellular nothofagin production obtained from the Escherichia coli strain ScCGT1-P164T reached 38 mg/L, which was 2.3-fold higher than that of the wild-type strain. Finally, it is proved that the coupling catalysis of CjFNS I/F2H and ScCGT1-P164T could convert naringenin into vitexin and isovitexin.
conclusionThis is the first time that C-glycosyltransferase has been characterized from fern species and provides a candidate gene and strategy for the efficient production of bioactive C-glycosides using enzyme catalysis and metabolic engineering.
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