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 >

Functions, structures, and applications of cellobiose 2-epimerase and glycoside hydrolase family 130 mannoside phosphorylases

Files in This Item:
Saburi_CE and GH130 revised(HUSCAP).pdf575.95 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/67482

Title: Functions, structures, and applications of cellobiose 2-epimerase and glycoside hydrolase family 130 mannoside phosphorylases
Authors: Saburi, Wataru Browse this author →KAKEN DB
Keywords: cellobiose 2-epimerase
4-O-β-d-mannosyl-d-glucose phosphorylase
β-1,4-mannooligosaccharide phosphorylase
glycoside hydrolase family 130
epilactose
Issue Date: Jul-2016
Publisher: Taylor & Francis
Journal Title: Bioscience, Biotechnology, and Biochemistry
Volume: 80
Issue: 7
Start Page: 1294
End Page: 1305
Publisher DOI: 10.1080/09168451.2016.1166934
PMID: 27031293
Abstract: Carbohydrate isomerases/epimerases are essential in carbohydrate metabolism, and have great potential in industrial carbohydrate conversion. Cellobiose 2-epimerase (CE) reversibly epimerizes the reducing end d-glucose residue of β-(1→4)-linked disaccharides to d-mannose residue. CE shares catalytic machinery with monosaccharide isomerases and epimerases having an (α/α)6-barrel catalytic domain. Two histidine residues act as general acid and base catalysts in the proton abstraction and addition mechanism. β-Mannoside hydrolase and 4-O-β-d-mannosyl-d-glucose phosphorylase (MGP) were found as neighboring genes of CE, meaning that CE is involved in β-mannan metabolism, where it epimerizes β-d-mannopyranosyl-(1→4)-d-mannose to β-d-mannopyranosyl-(1→4)-d-glucose for further phosphorolysis. MGPs form glycoside hydrolase family 130 (GH130) together with other β-mannoside phosphorylases and hydrolases. Structural analysis of GH130 enzymes revealed an unusual catalytic mechanism involving a proton relay and the molecular basis for substrate and reaction specificities. Epilactose, efficiently produced from lactose using CE, has superior physiological functions as a prebiotic oligosaccharide.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience, biotechnology, and biochemistry on 7/2016, available online: http://wwww.tandfonline.com/10.1080/09168451.2016.1166934.
Type: article (author version)
URI: http://hdl.handle.net/2115/67482
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_1.0 )

MathJax is now OFF:


 

 - Hokkaido University