ArticlePlant biotechnology journal2025
Molecular characterization and structural basis of a promiscuous glycosyltransferase for β-(1,6) oligoglucoside chain glycosides biosynthesis.
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 4 papers.
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4 citing papers in PubMed.
- Complete biosynthesis of the clinical agent escin Ia.Nature communications · 2026Article
- High-Resolution Mass Spectrometry Reveals Distinct Temporal Accumulation Patterns of Metabolites in Reproductive Organs of Purple- and White-FloweredLife (Basel, Switzerland) · 2026Article
- Efficient Synthesis of Glucovanillin and Elucidation of Its Molecular Mechanisms in Ameliorating T2DM via Core Target Modulation and α-Glucosidase Inhibition.Molecules (Basel, Switzerland) · 2026Article
- Structural insights into the catalytic mechanism of the phenylethanoid glycoside rhamnosyltransferase UGT79G15 from Rehmannia glutinosa.Plant communications · 2025Article
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9 authors.
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Abstract
Sugar building blocks are crucial for the chemical diversity and biological activity of secondary metabolites. UDP-dependent glycosyltransferases (UGTs) play a pivotal role in the biosynthesis of glycosides in plants by catalysing the attachment of sugar moieties to various bioactive natural products. However, the biosynthesis of oligosaccharide-chain glycosides is often limited by the narrow substrate specificity of UGTs. In this study, we identify a regio-specific β-(1,6) glycosyltransferase, UGT94BY1, from Platycodon grandiflorum. UGT94BY1 exhibits broad substrate promiscuity and can transfer up to three sugar moieties to the C6-OH position of the glucosyl group in various triterpenoids and phenolic glycosides, thereby forming β-(1,6) oligoglucoside chains. To elucidate the mechanism underlying its substrate selectivity, we determined the crystal structure of the UGT94BY1 complex with UDP at a resolution of 2.0 Å. Molecular simulations revealed that a critical structural motif, comprising residues N84-M91, S141-L155 and R179-E186, plays a key role in recognizing sugar acceptors and facilitating chain elongation. Our study unveils a powerful glycosyltransferase for β-(1,6) oligoglucoside chain biosynthesis and highlights key regions involved in substrate recognition and sugar chain extension, providing valuable insights for designing UGTs with customized substrate specificities for biotechnological applications.
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