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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

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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)

Submitter: 森 春英

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