Identification of novel demyristoylation enzyme controlling lipid modification cycle and its structural function analysis
Project/Area Number |
15K14712
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Applied biochemistry
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Research Institution | Kyoto Gakuen University |
Principal Investigator |
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Project Period (FY) |
2015-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
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Keywords | ミリストイル化 / ミリスチル化 / 脂質修飾 / 細胞内シグナル伝達 / 脱ミリストイル化酵素 / シグナル伝達 / 脱ミリストイル化 / 酵素 / クリックケミストリー |
Outline of Final Research Achievements |
Protein myristoylation is an irreversible lipid modification and demyristoylation enzymes have not yet been identified. Since many myristoylated proteins are important for disease pathogenesis, it is a major finding to clarify the presence of demyristoylation enzymes involved in the regulation of myristoylated proteins. In this study, we aimed to purify and identify the demyristoylation enzyme and to clarify its enzymatic caharacteristics. As a result, we succeeded in finding demyristoylation activity from rat brain soluble fraction. In this research process, we also developed an assay system to identify demytostroylation activity.
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Report
(4 results)
Research Products
(11 results)
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[Journal Article] Effectiveness of exersize-induced cytokines in alleviating arthritis sympotoms in arthritis model mice2016
Author(s)
Kito, T., Teranishi, T., Nishii, K., Sasaki, K., Matsubara, M., Yamada, K.
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Journal Title
Okajima Folia Anat. Jpn
Volume: 93
Pages: 81-88
Related Report
Peer Reviewed / Open Access
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