Substrate recognition of glucosidase II in ER and its related enzymes
Project/Area Number |
22780082
|
Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Applied biochemistry
|
Research Institution | Hokkaido University |
Principal Investigator |
|
Project Period (FY) |
2010 – 2011
|
Project Status |
Completed (Fiscal Year 2011)
|
Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2010: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
Keywords | α-グルコシダーゼ / 基質特異性 / 分子進化 / α-グルコシダーゼII / 立体構造解析 / 部位特異的変異 / 小胞体グルコシダーゼ / タンパク質の分子進化 / 基質認識 |
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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Report
(3 results)
Research Products
(39 results)