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多酵素カスケードのためのNAD(P) H依存人工転移ヒドロゲナーゼ
Yasunori Okamoto1, Valentin Köhler1, Thomas R Ward1
1Department of Chemistry, University of Basel , Spitalstrasse 51, CH-4056 Basel, Switzerland.
Journal of the American Chemical Society
|April 22, 2016
まとめ
研究者は,イミン減少のためにNAD (P) Hを使用する新しい人工転送ヒドロゲン酶 (ATHase) を開発した. この酵素は,グルコース脱水素酵素と結合して,マルチ酵素カスケードを通じて,効率的で持続的なアミンの合成を可能にします.
科学分野:
- 生物触媒
- 有機金属化学
- 酵素工学
背景:
- 伝統的な酵素は,減量のためにNAD (P) HまたはFADH2を使用します.
- オルガノメタリック触媒は一般的にイソプロパノールまたはホルマートを使用して,ヒドリドを生成します.
- 酵素化水素移転を模倣する新しい触媒が必要である.
研究 の 目的:
- NAD(P) H依存の人工転移ヒドロゲンゼ (ATHase) を設計する.
- イミンの減少におけるATHaseの触媒効率を証明する.
- エナチオピュアアミン生成のためのカスケード反応を開発する.
主な方法:
- バイオチンとジヒドロキシフェナントロリンとCp*Irコファクターをストレプタヴィジンに組み込む.
- 設計されたATHaseをNADPHでイミン還元に使用する.
- グルコース脱水素酵素 (GDH) とグルコースを用いたNADPHの同時再生.
- ATHase,GDH,モノアミン酸化酵素,カタラゼを含む4つの酵素のカスケードを構築する.
主要な成果:
- 低濃度のNADPHを用いてイミン減少を効率的に触媒化した.
- NADPHの再生は,GDHによるステキオメトリック量のグルコースを用いて達成された.
- 4つの酵素のカスケードで エナチオプアミンが成功しました
結論:
- 開発されたATHaseは,還元反応のための新しい生物触媒ツールです.
- カスケードシステムは,エナチオピュアアミンを合成するための持続可能なアプローチを提供します.
- この研究は,有機金属触媒と酵素ヒドリド転送を橋渡しする.
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