Structural andfunctional analysis of glycoside hydrolases with multiple catalytic domains.
| Project/Area Number |
22580092
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Osaka Prefecture University |
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Principal Investigator |
SUMITANI Jun-ichi 大阪府立大学, 大学院・生命環境科学研究科, 准教授 (10264813)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIMURA Shigenori 大阪府立大学, 大学院・生命環境科学研究科, 助教 (90244665)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | アミラーゼ / デンプン結合ドメイン / マルチ触媒ドメイン / 構造機能相関 / デンプン結合領域 |
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| Research Abstract |
In this study, we revealed the interactions between two catalytic domains (CD), starch-binding domains (SBD), and CD-SBD, respectively, by the experiments for enzymology and the analysis for structural biology, using cell-surface-associated amylase from Streptomyces corchorusiiand /-amylase from Paenibacillus polymyxa, suggesting that a protein hold multi CD shows better catalytic efficiency than a protein hold single CD.
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Report
(4 results)
Research Products
(28 results)
