ArticleScientific reports2018
Isolation and characterization of a multifunctional flavonoid glycosyltransferase from Ornithogalum caudatum with glycosidase activity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 30 citations in OpenAlex.
- Phytochemical Study and In Vitro Antioxidant Activity ofMolecules (Basel, Switzerland) · 2024Article
- Functional characterization, structural basis, and protein engineering of a rare flavonoid 2'-Acta pharmaceutica Sinica. B · 2024Article
- Biosynthesis of Apigenin Glucosides in EngineeredJournal of microbiology and biotechnology · 2024Article
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- Glycosyltransferases: Mining, engineering and applications in biosynthesis of glycosylated plant natural products.Synthetic and systems biotechnology · 2022Article
- Promiscuity and specificity of eukaryotic glycosyltransferases.Biochemical Society transactions · 2020Review
- OcUGT1-Catalyzing Glycodiversification of Steroids through Glucosylation and Transglucosylation Actions.Molecules (Basel, Switzerland) · 2020Article
- De novo sequencing of Bletilla striata (Orchidaceae) transcriptome and identification of genes involved in polysaccharide biosynthesis.Genetics and molecular biology · 2020Article
- Transcriptome-Wide Identification of an Aurone Glycosyltransferase with Glycosidase Activity fromGenes · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
Glycosyltransferases (GTs) are bidirectional biocatalysts catalyzing the glycosylation of diverse molecules. However, the extensive applications of GTs in glycosides formation are limited due to their requirements of expensive nucleotide diphosphate (NDP)-sugars or NDP as the substrates. Here, in an effort to characterize flexible GTs for glycodiversification of natural products, we isolated a cDNA, designated as OcUGT1 from Ornithogalum caudatum, which encoded a flavonoid GT that was able to catalyze the trans-glycosylation reactions, allowing the formation of glycosides without the additions of NDP-sugars or NDP. In addition, OcUGT1 was observed to exhibit additional five types of functions, including classical sugar transfer reaction and three reversible reactions namely NDP-sugar synthesis, sugars exchange and aglycons exchange reactions, as well as enzymatic hydrolysis reaction, suggesting OcUGT1 displays both glycosyltransferase and glycosidase activities. Expression profiles revealed that the expression of OcUGT1 was development-dependent and affected by environmental factors. The unusual multifunctionality of OcUGT1 broadens the applicability of OcUGT1, thereby generating diverse carbohydrate-containing structures.
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