2011 Fiscal Year Final Research Report
Substrate recognition of glucosidase II in ER and its related enzymes
| Project/Area Number |
22780082
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
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| Project Period (FY) |
2010 – 2011
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| Keywords | α-グルコシダーゼ / 基質特異性 / 分子進化 |
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| Research Abstract |
The purpose of this project was to clarify molecular evolution ofα-glucosidases distributed largely in organisms. An.-glucosidase, which hydrolyzesα-1, 3-glucosidic linkage in endoplasmic reticulum, also showed specificity forα-1, 4-glucosidic linkage. Structural studies of an.-glucosidase indicated that the loop structure, which covers the active pocket, was involved in substrate recognition. Trp residue in the active pocket of an yeast.-glucosidase had important role for substrate specificity. Novel.-glucosidase, which preferredα-1, 3-glucosidic linkage, was discovered from bacteria. It seems that an ancestor enzyme originally hadα-1, 3 specificity and its derivatives have acquired various specificity during the molecular evolution. Moreover, it appears that protein with a new function remained in the related family
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[Journal Article] Novel dextranase catalyzing cycloisomaltooligosaccharide-formation and identification of catalytic amino acids and their functions using chemical rescue approach2012
Author(s)
Kim YM, Kiso Y, Muraki T, Kang MS, Nakai H, Saburi W, LangW, Kang HK, Okuyama M, Mori H, Suzuki R, Funane K, Suzuki N, Momma M, Fujimoto Z, Oguma T, Kobayashi M, Kim D, Kimura A
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Journal Title
J Biol Chem
Volume: (印刷中)
DOI
Peer Reviewed
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