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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >
Functional reassignment of Cellvibrio vulgaris EpiA to cellobiose 2-epimerase and an evaluation of the biochemical functions of the 4-O-beta-d-mannosyl-d-glucose phosphorylase-like protein, UnkA
| Title: | Functional reassignment of Cellvibrio vulgaris EpiA to cellobiose 2-epimerase and an evaluation of the biochemical functions of the 4-O-beta-d-mannosyl-d-glucose phosphorylase-like protein, UnkA |
| Authors: | Saburi, Wataru Browse this author →KAKEN DB | | Tanaka, Yuka Browse this author | | Muto, Hirohiko Browse this author | | Inoue, Sota Browse this author | | Odaka, Rei Browse this author | | Nishimoto, Mamoru Browse this author | | Kitaoka, Motomitsu Browse this author | | Mori, Haruhide Browse this author →KAKEN DB |
| Keywords: | 4-O-beta-d-mannosyl-d-glucose phosphorylase | | substrate specificity | | Cellvibrio vulgaris | | beta-mannan | | cellobiose 2-epimerase |
| Issue Date: | 4-Jun-2015 |
| Publisher: | Taylor & Francis |
| Journal Title: | Bioscience biotechnology and biochemistry |
| Volume: | 79 |
| Issue: | 6 |
| Start Page: | 969 |
| End Page: | 977 |
| Publisher DOI: | 10.1080/09168451.2015.1012146 |
| PMID: | 25704402 |
| Abstract: | The aerobic soil bacterium Cellvibrio vulgaris has a beta-mannan-degradation gene cluster, including unkA, epiA, man5A, and aga27A. Among these genes, epiA has been assigned to encode an epimerase for converting d-mannose to d-glucose, even though the amino acid sequence of EpiA is similar to that of cellobiose 2-epimerases (CEs). UnkA, whose function currently remains unknown, shows a high sequence identity to 4-O-beta-d-mannosyl-d-glucose phosphorylase. In this study, we have investigated CE activity of EpiA and the general characteristics of UnkA using recombinant proteins from Escherichia coli. Recombinant EpiA catalyzed the epimerization of the 2-OH group of sugar residue at the reducing end of cellobiose, lactose, and beta-(1 -> 4)-mannobiose in a similar manner to other CEs. Furthermore, the reaction efficiency of EpiA for beta-(1 -> 4)-mannobiose was 5.5x10(4)-fold higher than it was for d-mannose. Recombinant UnkA phosphorolyzed beta-d-mannosyl-(1 -> 4)-d-glucose and specifically utilized d-glucose as an acceptor in the reverse reaction, which indicated that UnkA is a typical 4-O-beta-d-mannosyl-d-glucose phosphorylase. |
| Rights: | This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on [date of publication], available online: http://www.tandfonline.com/doi/abs/10.1080/09168451.2015.1012146?journalCode=tbbb20 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/62061 |
| Appears in Collections: | 農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 森 春英
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