| Project/Area Number |
21K19094
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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 38:Agricultural chemistry and related fields
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| Research Institution | Osaka Metropolitan University (2022)
Osaka Prefecture University (2021) |
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Principal Investigator |
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| Project Period (FY) |
2021-07-09 – 2023-03-31
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| Project Status |
Completed (Fiscal Year 2022)
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| Budget Amount *help |
¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
Fiscal Year 2022: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2021: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
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| Keywords | 補欠分子族 / 翻訳後化学修飾 / キノプロテイン / Protein-derived cofactor / 人工金属酵素 |
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| Outline of Research at the Start |
タンパク質に化学修飾して機能化を行う、簡単に言うとひとの力で少しお化粧直しを施してタンパク質のいろいろな顔を引き出す研究になります。もしこれができると、日常生活での酵素タンパク質の利用方法の拡充や医薬品開発のもとになる細胞内でのタンパク質の役割解明など様々な成果が得られます。本研究はこうした手法のうち、天然のタンパク質が持つ修飾方法を発展させて全自動で行わせる方法を模索するものです。
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| Outline of Final Research Achievements |
Recently, the development of analytical techniques has led to the discovery of novel built-in coenzymes formed by post-translational chemical modification of amino acid residues in proteins, such as cysteinyl tyrosine in galactose oxidase (GAO). In our laboratory, we have studied the cupin protein from thermophilic bacteria, which has low molecular weight and a metal binding motif with four histidines. In this study, we prepared a copper-containing metalloprotein that mimics the environment of the active center of GAO by using this protein, and formed a Tyr-Cys cross-linked structure using this protein. Thus, by using saturated mutagenesis to two amino acid residues in the proximity of Tyr108, the crosslink formation of these mutant was further improved.
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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として高度な機能を発揮するものがある。その機能は様々で他の有機補因子やカノニカルなアミノ酸残基にはない物理化学・触媒化学的に珍しい性質を示す。このように、今後、本研究結果を発展させ、様々な特殊なアミノ酸残基を形成させることができ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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