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Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe

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Title: Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe
Authors: Okuyama, Masayuki Browse this author →KAKEN DB
Miyamoto, Masashi Browse this author
Matsuo, Ichiro Browse this author
Iwamoto, Shogo Browse this author
Serizawa, Ryo Browse this author
Tanuma, Masanari Browse this author
Ma, Min Browse this author
Klahan, Patcharapa Browse this author
Kumagai, Yuya Browse this author
Tagami, Takayoshi Browse this author
Kimura, Atsuo Browse this author →KAKEN DB
Keywords: catalytic alpha-subunit of ER glucosidase II
heterologous expression
glycoside hydrolase family 31
substrate specificity
Issue Date: Aug-2017
Publisher: Taylor & Francis
Journal Title: Bioscience biotechnology and biochemistry
Volume: 81
Issue: 8
Start Page: 1503
End Page: 1511
Publisher DOI: 10.1080/09168451.2017.1320520
PMID: 28471318
Abstract: The recombinant catalytic alpha-subunit of N-glycan processing glucosidase II from Schizosaccharomyces pombe (SpGII alpha) was produced in Escherichia coli. The recombinant SpGII alpha exhibited quite low stability, with a reduction in activity to <40% after 2-days preservation at 4 degrees C, but the presence of 10% (v/v) glycerol prevented this loss of activity. SpGII alpha, a member of the glycoside hydrolase family 31 (GH31), displayed the typical substrate specificity of GH31 alpha-glucosidases. The enzyme hydrolyzed not only alpha-(1 -> 3)-but also alpha-(1 -> 2)-, alpha-(1 -> 4)-, and alpha-(1 -> 6)-glucosidic linkages, and p-nitrophenyl alpha-glucoside. SpGII alpha displayed most catalytic properties of glucosidase II. Hydrolytic activity of the terminal alpha-glucosidic residue of Glc(2)Man(3)-Dansyl was faster than that of Glc(1)Man(3)-Dansyl. This catalytic alpha-subunit also removed terminal glucose residues from native N-glycans (Glc(2)Man(9)GlcNAc(2) and Glc(1)Man(9)GlcNAc(2)) although the activity was low.
Rights: This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 2017 Aug, 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: 奥山 正幸

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