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Journal article

Natural product C-glycosyltransferases - a scarcely characterised enzymatic activity with biotechnological potential

From

Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark1

Enzyme Engineering & Structural Biology, Research Groups, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark2

Enzyme and Protein Chemistry, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark3

Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark4

Covering: up to 2020C-Glycosyltransferases are enzymes that catalyse the transfer of sugar molecules to carbon atoms in substituted aromatic rings of a variety of natural products. The resulting β-C-glycosidic bond is more stable in vivo than most O-glycosidic bonds, hence offering an attractive modulation of a variety of compounds with multiple biological activities.

While C-glycosylated natural products have been known for centuries, our knowledge of corresponding C-glycosyltransferases is scarce. Here, we discuss commonalities and differences in the known C-glycosyltransferases, review attempts to leverage them as synthetic biocatalysts, and discuss current challenges and limitations in their research and application.

Language: English
Publisher: The Royal Society of Chemistry
Year: 2021
Pages: 432-443
ISSN: 14604752 and 02650568
Types: Journal article
DOI: 10.1039/d0np00040j
ORCIDs: Putkaradze, Natalia , Tezé, David , Fredslund, Folmer and Welner, Ditte Hededam

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