| Project/Area Number |
23570132
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Tokyo University of Agriculture and Technology |
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Principal Investigator |
TONOZUKA Takashi 東京農工大学, (連合)農学研究科(研究院), 准教授 (50285194)
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| Co-Investigator(Renkei-kenkyūsha) |
NISHIKWA Atsushi 東京農工大学, 大学院農学研究院, 教授 (30218127)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2011: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 酵素 / 糖 / 糖質加水分解酵素 / グリコシンターゼ / 糖タンパク質糖鎖 / X線結晶構造解析 / グルコシダーゼ / 糖質加水分解酵素ファミリー63 / オリゴ糖 / Ｘ線結晶構造解析 / マンノシダーゼ |
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| Research Abstract |
This study focuses on bacterial enzymes homologous to processing alpha-glucosidases I and II, both of which hydrolyze eukaryotic glycans. An enzyme from E. coli, YgjK, was successfully converted into a glycosynthase, and the enzyme efficiently produced Glc-alpha-1,2-Gal. The result suggests that the natural substrates of YgjK are likely to be sugars containing the Glc-alpha-1,2-Gal structure. We also studied related enzymes from Thermus and other bacterial species. This study shows that a combination of protein crystallography and glycosynthase reaction allows us to determine the natural substrates of carbohydrate-active enzymes, even if the substrates are not commercially available.
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