Domain-Swapping of a GT-B Glycosyltransferase Broadens Its Sugar Donor Range for Glycodiversification of Natural Products
Abstract
Glycosylation of natural compounds modulates their bioactivity as well as their physicochemical properties, making glycodiversification a valuable strategy for identifying glycosidic derivatives with improved functional profiles. However, the use of glycosyltransferases (GTs) for their synthesis is constrained by stringent sugar nucleotide donor selectivity, which limits the structural diversity of accessible glycosides. The chimeric NB1//CC1, constituted of 2 self-assembled domains originating from plant glycosyltransferases, was previously demonstrated to transfer glucose onto a wider range of natural compounds than its parental enzymes. This study demonstrates that this chimeric enzyme also exhibits a relaxed selectivity toward sugar nucleotide donors. This donor promiscuity can further be enhanced by the Mg2+ cation, which increases the sugar transfer rate for the chimeric enzyme. NB1//CC1 can therefore be used as a single biocatalyst to generate a library of glycosidic variants of a given natural glycosylated compound.
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BibTeX
@article{gilleron2026domainswapping,
title = {{Domain-Swapping of a GT-B Glycosyltransferase Broadens Its Sugar Donor Range for Glycodiversification of Natural Products}},
author = {Caroline Gilleron and Arnaud Pâris and Ilham Alloui and Tiffany Rundstadler and Laëtitia Fougère and Malika Mekhalfi and Pierre Lafite},
journal = {Journal of Agricultural and Food Chemistry},
year = {2026},
month = aug,
doi = {10.1021/acs.jafc.6c10592},
url = {https://hal.science/hal-05736638v1},
note = {CC BY-NC 4.0},
}
RIS
TY - JOUR
TI - Domain-Swapping of a GT-B Glycosyltransferase Broadens Its Sugar Donor Range for Glycodiversification of Natural Products
AU - Caroline Gilleron
AU - Arnaud Pâris
AU - Ilham Alloui
AU - Tiffany Rundstadler
AU - Laëtitia Fougère
AU - Malika Mekhalfi
AU - Pierre Lafite
PY - 2026
DA - 2026/08/31
JO - Journal of Agricultural and Food Chemistry
DO - 10.1021/acs.jafc.6c10592
UR - https://hal.science/hal-05736638v1
AB - Glycosylation of natural compounds modulates their bioactivity as well as their physicochemical properties, making glycodiversification a valuable strategy for identifying glycosidic derivatives with improved functional profiles. However, the use of glycosyltransferases (GTs) for their synthesis is constrained by stringent sugar nucleotide donor selectivity, which limits the structural diversity of accessible glycosides. The chimeric NB1//CC1, constituted of 2 self-assembled domains originating from plant glycosyltransferases, was previously demonstrated to transfer glucose onto a wider range of natural compounds than its parental enzymes. This study demonstrates that this chimeric enzyme also exhibits a relaxed selectivity toward sugar nucleotide donors. This donor promiscuity can further be enhanced by the Mg2+ cation, which increases the sugar transfer rate for the chimeric enzyme. NB1//CC1 can therefore be used as a single biocatalyst to generate a library of glycosidic variants of a given natural glycosylated compound.
SN - 0021-8561
SN - 1520-5118
ER -