2015年6月
Functional reassignment of Cellvibrio vulgaris EpiA to cellobiose 2-epimerase and an evaluation of the biochemical functions of the 4-O-β-D-mannosyl-D-glucose phosphorylase-like protein, UnkA
Bioscience, Biotechnology and Biochemistry
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- 巻
- 79
- 号
- 6
- 開始ページ
- 969
- 終了ページ
- 977
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1080/09168451.2015.1012146
© 2015 Japan Society for Bioscience, Biotechnology, and Agrochemistry.The aerobic soil bacterium Cellvibrio vulgaris has a β-mannan-degradation gene cluster, including unkA, epiA, man5A, and aga27A. Among these genes, epiA has been assigned to encode an epimer-ase 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-β-D-mannosyl-D-glu-cose 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 β-(1→4)-mannobiose in a similar manner to other CEs. Furthermore, the reaction efficiency of EpiA for β-(1→4)-mannobiose was 5.5 × 10<sup>4</sup>-fold higher than it was for D-mannose. Recombinant UnkA phosphorolyzed β-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-β-D-mannosyl-D-glucose phosphorylase.
- リンク情報
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- DOI
- https://doi.org/10.1080/09168451.2015.1012146
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/25704402
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000356239400014&DestApp=WOS_CPL
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84940032549&origin=inward
- ID情報
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- DOI : 10.1080/09168451.2015.1012146
- ISSN : 0916-8451
- eISSN : 1347-6947
- PubMed ID : 25704402
- SCOPUS ID : 84940032549
- Web of Science ID : WOS:000356239400014