ArticleNature communications2024
An efficient C-glycoside production platform enabled by rationally tuning the chemoselectivity of glycosyltransferases.
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 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structure-coevolution dual-guided engineering of C-glycosyltransferase enables high-level biosynthesis of vitexin inSynthetic and systems biotechnology · 2026Article
- Integrated metabolomic and transcriptomic analysis of Camellia sinensis var. pubilimba 'Rucheng Baimaocha' reveals distinct flavonoid and strictinin biosynthesis.BMC plant biology · 2026Article
- A breakthrough in synthetic biology: industrial scaling-up flavonoid C-glycoside production in yeast.Science China. Life sciences · 2026Article
- Tuning aromatic cage occupancy in prenyltransferases enables selective and efficient production of rare c-prenylated flavonoids.Nature communications · 2026Article
- Tailoring Regioselectivity-Controlled UDP-Glycosyltransferase for Bidirectional Glycosylation of Tyrosol via Free Energy-Driven Pocket Reshaping and Tunnel Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mechanistic elucidation of enzymaticRSC advances · 2025Article
- One-Pot Hetero-Di-C-Glycosylation of the Natural Polyphenol Phloretin by a Single C-Glycosyltransferase With Broad Sugar Substrate Specificity.Biotechnology and bioengineering · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Despite the broad potential applications of C-glycosides, facile synthetic methods remain scarce. Transforming glycosyltransferases with promiscuous or natural O-specific chemoselectivity to C-glycosyltransferases is challenging. Here, we employ rational directed evolution of the glycosyltransferase MiCGT to generate MiCGT-QDP and MiCGT-ATD mutants which either enhance C-glycosylation or switch to O-glycosylation, respectively. Structural analysis and computational simulations reveal that substrate binding mode govern C-/O-glycosylation selectivity. Notably, directed evolution and mechanism analysis pinpoint the crucial residues dictating the binding mode, enabling the rational design of four enzymes with superior non-inherent chemoselectivity, despite limited sequence homology. Moreover, our best mutants undergo testing with 34 substrates, demonstrating superb chemoselectivities, regioselectivities, and activities. Remarkably, three C-glycosides and an O-glycoside are produced on a gram scale, demonstrating practical utility. This work establishes a highly selective platform for diverse glycosides, and offers a practical strategy for creating various types of glycosylation platforms to access pharmaceutically and medicinally interesting products.
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