Elucidation of mobile loop functions in food-related enzymes
| Project/Area Number |
21380064
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
MIKAMI Bunzo 京都大学, 大学院・農学研究科, 教授 (40135611)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000)
Fiscal Year 2011: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2010: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2009: ¥10,140,000 (Direct Cost: ¥7,800,000、Indirect Cost: ¥2,340,000)
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| Keywords | タンパク質工学 / 応用構造生物学 / X線結晶構造解析 / 酵素反応機構 / 酵素 / タンパク質構造変化 / フレキシブルループ / 酵素反応 / 構造生物学 |
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| Research Abstract |
The functions of proteins are usually expressed by conformational changes in loop regions. We have investigated the mobile loops in food-related enzymes that are used in food industry. The mobile loops in the active sites of.-amylase and alginate lyase that are important for incorporation of substrate and release of product are analyzed by X-ray crystal analyses of their mutant enzymes. In order to reveal the enzyme mechanism of protein-glutaminase, a mutant of pro protein-glutaminase(A47Q) was prepared. It was found that the mutated Gln47 formed Michaelis complex and S-acyl covalent intermediate with a catalytic cysteine residue.
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Report
(4 results)
Research Products
(22 results)
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[Journal Article]2010
Author(s)
三上文三, 丸山伸之, 内海成
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Journal Title
大豆のすべて (喜多村啓介他編集) 第4章2節2 グロブリンタンパク質(サイエンスフォーラム)
Pages: 115-121
Related Report
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