| 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)
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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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