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Cu II ‐Containing 1‐Aminocyclopropane Carboxylic Acid Oxidase Is an Efficient Stereospecific Diels–Alderase
Author(s) -
Ghattas Wadih,
Dubosclard Virginie,
Tachon Sybille,
Beaumet Morane,
Guillot Régis,
Réglier Marius,
Simaan A. Jalila,
Mahy JeanPierre
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201909407
Subject(s) - stereospecificity , chemistry , cyclopentadiene , cycloaddition , enzyme , stereochemistry , catalysis , yield (engineering) , oxidase test , context (archaeology) , enzyme catalysis , natural product , organic chemistry , materials science , biology , paleontology , metallurgy
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 II served as an efficient artificial Diels–Alderase. The kinetic parameters of the catalysis of the cycloaddition of cyclopentadiene and 2‐azachalcone were determined ( K M =230 μ m , k app =3 h −1 ), which gave access to reaction conditions that provided quantitative yield and >99 % ee of the ( 1S , 2R , 3R , 4R ) 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 ( 1S , 2R , 3R , 4R ) product isomer.