Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 서주현 | * |
dc.date.accessioned | 2016-08-29T12:08:14Z | - |
dc.date.available | 2016-08-29T12:08:14Z | - |
dc.date.issued | 2015 | * |
dc.identifier.issn | 20452322 | * |
dc.identifier.other | OAK-15168 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/230651 | - |
dc.description.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. | * |
dc.language | English | * |
dc.publisher | Nature Publishing Group | * |
dc.title | Characterization of two-step deglycosylation via oxidation by glycoside oxidoreductase and defining their subfamily | * |
dc.type | Article | * |
dc.relation.volume | 5 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.journaltitle | Scientific Reports | * |
dc.identifier.doi | 10.1038/srep10877 | * |
dc.identifier.scopusid | 2-s2.0-84931282162 | * |
dc.author.google | Kim E.-M. | * |
dc.author.google | Seo J.-H. | * |
dc.author.google | Baek K. | * |
dc.author.google | Kim B.-G. | * |
dc.contributor.scopusid | 서주현(34771833400) | * |
dc.date.modifydate | 20240322121534 | * |