Rational design of artificial radical enzymes bearing unusual protein-derived cofactor
| Project/Area Number |
18K19151
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 37:Biomolecular chemistry and related fields
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| Research Institution | Osaka Prefecture University |
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Principal Investigator |
Fujieda Nobutaka 大阪府立大学, 生命環境科学研究科, 准教授 (00452318)
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| Project Period (FY) |
2018-06-29 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2019: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2018: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
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| Keywords | 翻訳後化学修飾 / 補欠分子族 / キノプロテイン / Protein-derived cofactor / 人工金属酵素 / 自己水酸化 / ラジカル酵素 |
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| Outline of Final Research Achievements |
Galactose oxidase and amine oxidase bear the cofactors which is generated by post-translationally chemical modification of the corresponding amino acid side chains near the copper active center. For example, galactose oxidase has a cysteinyl-tyrosine (Cys－Tyr) cofactor formed from cysteine and tyrosine. The Cys－Tyr cofactor generates radical species as a reactive intermediate in the catalytic oxidation of alcohols. In this study, we have prepared rationally designed copper-binding proteins, which can induce the organic cofactors by posttranslationally chemical modifications. The structures and redox functions of the generated cofactors in the proteins were explored by several spectroscopic methods including X-ray crystallographic analysis.
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| Academic Significance and Societal Importance of the Research Achievements |
芳香族アミノ酸から生じる特殊な側鎖は配位子や補欠分子族(Protein-derived cofactor (PDC))として機能中枢を司るものが多く、その機能は多種多様で他の有機補因子にはない物理化学・触媒化学的に稀有な性質を示す。このように、今後、本研究結果を発展させ、様々なPDCを形成させることが可能になればタンパク質のさらなる機能化が期待される。
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Report
(4 results)
Research Products
(20 results)
