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Characterization of two-step deglycosylation via oxidation by glycoside oxidoreductase and defining their subfamily
- Title
- Characterization of two-step deglycosylation via oxidation by glycoside oxidoreductase and defining their subfamily
- Authors
- Kim E.-M.; Seo J.-H.; Baek K.; Kim B.-G.
- Ewha Authors
- 서주현
- SCOPUS Author ID
- 서주현
- Issue Date
- 2015
- Journal Title
- Scientific Reports
- ISSN
- 20452322
- Citation
- Scientific Reports vol. 5
- Publisher
- Nature Publishing Group
- Indexed
- SCI; SCIE; SCOPUS
- Document Type
- Article
- 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. © 2015, Nature Publishing Group. All rights reserved.
- DOI
- 10.1038/srep10877
- Appears in Collections:
- 공과대학 > 식품생명공학과 > Journal papers
- Files in This Item:
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