酸化性N-デメチラーゼは,どこにでもあるセンサーから酵素へのPAS移行を明らかにする
Mary Ortmayer1, Pierre Lafite1, Binuraj R K Menon1
1Manchester Institute of Biotechnology, School of Chemistry, 131 Princess Street, University of Manchester, Manchester M1 7DN, UK.
Nature
|November 17, 2016
まとめ
研究 者 たち は,多用途 の タンパク質 モジュール で ある Per-ARNT-Sim (PAS) ドメイン を 備えた 最初の 酵素 を 発見 し まし た. この新しい酵素はディメチラミンを酸化し,PASドメインを示しています.
科学分野:
- 生物化学
- 酵素学
- 構造生物学
背景:
- Per-ARNT-Sim (PAS) ドメインは,様々な環境シグナルを感知する保存されたシグナリングモジュールです.
- PASドメインはヘムやフラビンなどの様々なリンガンを結合しますが,酵素の活性については以前は知られていませんでした.
- PASの構造的多用途性は,触媒機能の可能性を示唆しています.
研究 の 目的:
- 最初に特定された酵素性PASドメインを特徴づける.
- 新しいヘム依存性酸化性N-デメチラーゼのメカニズムを解明する.
- PASの触媒の可能性を探るため
主な方法:
- 新しい酵素の生化学的特徴
- PASドメインの構造分析
- 基板による酸素活性化の調査
主要な成果:
- ヘム依存性酸化性N-デメチラーゼである最初の酵素性PASドメインを特定し,特徴づけました.
- 酵素はヘム,フラビンモノヌクレオチド,2Fe-2S,およびテトラヒドロフォリック酸の共因子を利用する.
- 構造データによると,PASドメインはヘムと基板に結合し,酸素の活性化を促進します.
結論:
- PASドメインはセンサから酵素に移行できます.
- この発見は,どこにでも存在するPASの機能を拡張します.
- PASの適応性は人工酵素の設計の可能性を示唆しています
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