ArticleScientific reports2015
Characterization of two-step deglycosylation via oxidation by glycoside oxidoreductase and defining their subfamily.
Article in Scientific reports, 2015. 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, 16 citations in OpenAlex.
- Characterization of the initial degradation mechanism involved inApplied and environmental microbiology · 2025Article
- Evolution and separation of actinobacterial pyranose andApplied and environmental microbiology · 2024Article
- Glycoside-metabolizing oxidoreductase D3dgpA from human gut bacterium.Frontiers in bioengineering and biotechnology · 2024Article
- Mechanistic insights into glycoside 3-oxidases involved in C-glycoside metabolism in soil microorganisms.Nature communications · 2023Article
- Enzymatic β-elimination in natural product O- and C-glycoside deglycosylation.Nature communications · 2023Article
- Theoretical study on the glycosidic C-C bond cleavage of 3''-oxo-puerarin.Scientific reports · 2023Article
- C-Glycoside metabolism in the gut and in nature: Identification, characterization, structural analyses and distribution of C-C bond-cleaving enzymes.Nature communications · 2021Article
- FAD-dependentProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Deglycosylation of the IsoflavoneApplied and environmental microbiology · 2020Article
- Comparative Genomics and CAZyme Genome Repertoires of MarineMarine drugs · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herein, we report a two-step deglycosylation mediated by the oxidation of glycoside which is different from traditional glycoside hydrolase (GH) mechanism. Previously, we reported a novel flavin adenine dinucleotide (FAD)-dependent glycoside oxidoreductase (FAD-GO) having deglycosylation activity. Various features of the reaction of FAD-GO such as including mechanism and catalytic residue and substrate specificity were studied. In addition, classification of novel FAD-GO subfamily was attempted. Deglycosylation of glycoside was performed spontaneously via oxidation of 3-OH of glycone moiety by FAD-GO mediated oxidation reaction. His493 residue was identified as a catalytic residue for the oxidation step. Interestingly, this enzyme has broad glycone and aglycon specificities. For the classification of FAD-GO enzyme subfamily, putative FAD-GOs were screened based on the FAD-GO from Rhizobium sp. GIN611 (gi 365822256) using BLAST search. The homologs of R. sp. GIN611 included the putative FAD-GOs from Stenotrophomonas strains, Sphingobacterium strains, Agrobacterium tumefaciens str. C58, and etc. All the cloned FAD-GOs from the three strains catalyzed the deglycosylation via enzymatic oxidation. Based on their substrate specificities, deglycosylation and oxidation activities to various ginsenosides, the FAD-GO subfamily members can be utilized as novel biocatalysts for the production of various aglycones.
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