Cu<sup>II</sup>‐Containing 1‐Aminocyclopropane Carboxylic Acid Oxidase Is an Efficient Stereospecific Diels–Alderase

DOI Web Site Web Site Web Site 被引用文献4件
  • Wadih Ghattas
    Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182 CNRS – Univ Paris Sud Université Paris-Saclay Orsay 91405 Cedex France
  • Virginie Dubosclard
    Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182 CNRS – Univ Paris Sud Université Paris-Saclay Orsay 91405 Cedex France
  • Sybille Tachon
    Institut des Sciences Moléculaires de Marseille (iSm2), UMR 7313 CNRS – Aix Marseille Univ Centrale Marseille Marseille 13013 Cedex France
  • Morane Beaumet
    Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182 CNRS – Univ Paris Sud Université Paris-Saclay Orsay 91405 Cedex France
  • Régis Guillot
    Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182 CNRS – Univ Paris Sud Université Paris-Saclay Orsay 91405 Cedex France
  • Marius Réglier
    Institut des Sciences Moléculaires de Marseille (iSm2), UMR 7313 CNRS – Aix Marseille Univ Centrale Marseille Marseille 13013 Cedex France
  • A. Jalila Simaan
    Institut des Sciences Moléculaires de Marseille (iSm2), UMR 7313 CNRS – Aix Marseille Univ Centrale Marseille Marseille 13013 Cedex France
  • Jean‐Pierre Mahy
    Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), UMR 8182 CNRS – Univ Paris Sud Université Paris-Saclay Orsay 91405 Cedex France

書誌事項

公開日
2019-09-05
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1002/anie.201909407
公開者
Wiley

この論文をさがす

説明

<jats:title>Abstract</jats:title><jats:p>In the context of developing ecofriendly chemistry, artificial enzymes are now considered as promising tools for synthesis. They are prepared in particular with the aim to catalyze reactions that are rarely, if ever, catalyzed by natural enzymes. We discovered that 1‐aminocyclopropane carboxylic acid oxidase reconstituted with Cu<jats:sup>II</jats:sup> served as an efficient artificial Diels–Alderase. The kinetic parameters of the catalysis of the cycloaddition of cyclopentadiene and 2‐azachalcone were determined (<jats:italic>K</jats:italic><jats:sub>M</jats:sub>=230 μ<jats:sc>m</jats:sc>, <jats:italic>k</jats:italic><jats:sub>app</jats:sub>=3 h<jats:sup>−1</jats:sup>), which gave access to reaction conditions that provided quantitative yield and >99 % <jats:italic>ee</jats:italic> of the (<jats:italic>1S</jats:italic>,<jats:italic>2R</jats:italic>,<jats:italic>3R</jats:italic>,<jats:italic>4R</jats:italic>) product isomer. This unprecedented performance was rationalized by molecular modeling as only one docking pose of 2‐azachalcone was possible in the active site of the enzyme and this was the one that leads to the (<jats:italic>1S</jats:italic>,<jats:italic>2R</jats:italic>,<jats:italic>3R</jats:italic>,<jats:italic>4R</jats:italic>) product isomer.</jats:p>

収録刊行物

被引用文献 (4)*注記

もっと見る

問題の指摘

ページトップへ