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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
서주현scopusscopus
Issue Date
2015
Journal Title
Scientific Reports
ISSN
20452322JCR Link
Citation
vol. 5
Publisher
Nature Publishing Group
Indexed
SCI; SCIE; SCOPUS scopus
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
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엘텍공과대학 > 식품공학전공 > Journal papers
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