| Project/Area Number |
24658092
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Gifu University |
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Principal Investigator |
EBIHARA Akio 岐阜大学, 応用生物科学部, 准教授 (60415099)
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| Co-Investigator(Renkei-kenkyūsha) |
OHNO Satoshi 岐阜大学, 工学部, 助教 (10345796)
KAMATARI Yuji O. 岐阜大学, 生命科学総合研究支援センター, 助教 (70342772)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2014: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | プロレニン / プロ酵素 / レニン / レニン・アンジオテンシン系 / 血圧調節 / 酵素化学 |
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| Outline of Final Research Achievements |
In our body, protease or a proteolytic enzyme is synthesized as a proenzyme that attaches an extra-sequence compared with the mature enzyme. The extra-sequence functions as a "safety lock", which prevents an unwanted burst of enzymatic activity. The aim of this study is to clarify the role of the safety lock that works in the proenzyme of renin, a key enzyme for regulating of blood pressure in our body. To date, no high-resolution structural information is available for renin in complex with its substrate. To improve the resolution of the complex structure, we planned to prepare a tight complex by an ultraviolet-cross linking. We succeeded in preparing a substrate protein where a non-natural amino acid suitable for the cross-linking is incorporated. In addition, we detected the complex formation via cross-linking reaction. This new preparation with a non-natural and photo-reactive amino acid would be a useful tool for understanding an inactivation mechanism of renin.
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