パートナー酸化酵素によってシトゥで生成されるアシクリルイミノ酸を遮断する非対称的還元酵素
Jin Guo1, Melanie A Higgins1, Phillip Daniel-Ivad1
1Department of Chemistry , University of British Columbia , Vancouver , British Columbia V6T 1Z4 , Canada.
Journal of the American Chemical Society
|July 13, 2019
まとめ
この研究は,不安定なアシクリルイミノ酸をキラルアミンに変換するイミノ酸還元酵素であるBsp5を特徴づけています. この発見は,d-アミノ酸の生物触媒合成のための新しい道を開きます.
科学分野:
- 生物化学
- 構造生物学
- 酵素学
背景:
- アサイクリックイミンは水性環境では化学的に不安定であり,バイオカタリシスでの使用を制限する.
- 既存のイミン還元酵素は,主に安定したサイクルイミンを処理し,多様なキラルアミンの合成を制限する.
研究 の 目的:
- 新しいイミノ酸還元酵素Bsp5の生化学的および構造的特徴を特定する.
- アサイクリックイミノ酸に対するBsp5の作用の構造的根拠を解明する.
- 生物触媒の応用における Bsp5 の可能性を調査する.
主な方法:
- 1.6 Åの解像度でd-アルギニンとNADPHとの複合体でBsp5の構造を決定するX線結晶学.
- サイト・ダイレクト・ミュータジェネシスで,酵素活性に関する重要な残留物を特定する.
- Bsp5の還元酵素活性を特徴付けるための生化学的測定
主要な成果:
- Bsp5の詳細な生化学的および構造的データは,d-2-ヒドロキシ酸脱水素酶の一族のイミノ酸還元酵素である.
- Bsp5のイミン削減活動のための最小構造要求の特定
- Bsp5が代替オキシダースパートナーの製品を処理でき,より広い基板の範囲を可能にすることを実証する.
結論:
- Bsp5は,パートナー酸化酵素によって*in situ*生成されるアサイクリックイミノ酸を効率的に減少させる.
- 構造的な洞察は,強化された生物触媒機能のためのBsp5のエンジニアリングのための基盤を提供します.
- Bsp5酸化系は,L-アミノ酸をD-アミノ酸に生物触媒的に変換する可能性を秘めている.
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