HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >

Characterization of a thermophilic 4-O-β-d-mannosyl-d-glucose phosphorylase fromRhodothermus marinus

Files in This Item:
131224_RmCE(HUSCAP).pdf479.06 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Characterization of a thermophilic 4-O-β-d-mannosyl-d-glucose phosphorylase fromRhodothermus marinus
Authors: Jaito, Nongluck Browse this author
Saburi, Wataru Browse this author →KAKEN DB
Odaka, Rei Browse this author
Kido, Yusuke Browse this author
Hamura, Ken Browse this author
Nishimoto, Mamoru Browse this author
Kitaoka, Motomitsu Browse this author
Matsui, Hirokazu Browse this author →KAKEN DB
Mori, Haruhide Browse this author →KAKEN DB
Keywords: Rhodothermus marinus
4-O-β-d-mannosyl-d-glucose phosphorylase
substrate specificity
Issue Date: 2014
Publisher: Taylor & Francis
Journal Title: Bioscience, Biotechnology, and Biochemistry
Volume: 78
Issue: 2
Start Page: 263
End Page: 270
Publisher DOI: 10.1080/09168451.2014.882760
PMID: 25036679
Abstract: 4-O-β-d-Mannosyl-d-glucose phosphorylase (MGP), found in anaerobes, converts 4-O-β-d-mannosyl-d-glucose (Man-Glc) to α-d-mannosyl phosphate and d-glucose. It participates in mannan metabolism with cellobiose 2-epimerase (CE), which converts β-1,4-mannobiose to Man-Glc. A putative MGP gene is present in the genome of the thermophilic aerobe Rhodothermus marinus (Rm) upstream of the gene encoding CE. Konjac glucomannan enhanced production by R. marinus of MGP, CE, and extracellular mannan endo-1,4-β-mannosidase. Recombinant RmMGP catalyzed the phosphorolysis of Man-Glc through a sequential bi–bi mechanism involving ternary complex formation. Its molecular masses were 45 and 222 kDa under denaturing and nondenaturing conditions, respectively. Its pH and temperature optima were 6.5 and 75 °C, and it was stable between pH 5.5–8.3 and below 80 °C. In the reverse reaction, RmMGP had higher acceptor preferences for 6-deoxy-d-glucose and d-xylose than R. albus NE1 MGP. In contrast to R. albus NE1 MGP, RmMGP utilized methyl β-d-glucoside and 1,5-anhydro-d-glucitol as acceptor substrates.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 2014, available online:
Type: article (author version)
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: 佐分利 亘

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


Feedback - Hokkaido University