| 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: http://www.tandfonline.com/10.1080/09168451.2017.1320520. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/71180 |
| 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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