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Functions, structures, and applications of cellobiose 2-epimerase and glycoside hydrolase family 130 mannoside phosphorylases
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)
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Submitter: 佐分利 亘
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