シアノバクチン生物合成における翻訳後のチロシンゲラニレーション
Maho Morita1, Yue Hao2, Jouni K Jokela3
1Department of Medicinal Chemistry , University of Utah , Salt Lake City , Utah 84112 , United States.
Journal of the American Chemical Society
|April 28, 2018
まとめ
研究者たちは新しい酵素 PirF を発見し,ピリサイクラミドのチロシンに C10 ゲラニル群を添加した. この前例のないOゲラニレーションは,薬剤発見における潜在的な応用を持つ新しい翻訳後の修正です.
科学分野:
- 生物化学
- 自然製品化学
- 合成生物学
背景:
- プレニレーションは二次代謝物質の活性を高め,シアノバクチンの生物合成に不可欠です.
- シアノバクチンアミノ酸は,通常,ABBAプレニルトランスフェラーゼによってC5ドナーを使用してイソプレニル化されます.
- シアノバクテリアによって生成されるピリサイクラミドは,C10ゲラニル基を含有することが示唆された.
研究 の 目的:
- ピリシクラミド生物合成に関与する新しいゲラニルトランスフェラーゼを特徴付ける.
- 前例のない Tyr O-ゲラニル化改変を調査する
- ピリシクラミド生物合成の構造と地域選択性を明らかにする.
主な方法:
- 酵素の浄化と特徴づけ
- 質量スペクトル分析
- 分析化学のテクニック
主要な成果:
- 新しいゲラニルトランスフェラーゼ (PirF) を特定し,浄化した.
- PirFがTyr O- ゲラニレーションを触媒化することを示した.これは前例のない翻訳後の変化である.
- ピリシクラミド7005E1の構造とPirFの地域選択性を決定した.
結論:
- PirFは,ピリシクラミドのバイオシンセシスにおける新しいTyr O-ゲラニレーションを触媒化する.
- この修正は,RiPPの翻訳後の修正の既知のレパートリーを拡張します.
- PirFは薬のような分子開発のための合成生物学のツールとして潜在しています.
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