Whole‐Cell Biocatalysts for Stereoselective C−H Amination Reactions. Issue 4 (21st December 2015)

• Record Type: Journal Article
• Authors: Both, Peter; Busch, Hanna; Kelly, Paul P.; Mutti, Francesco G.; Turner, Nicholas J.; Flitsch, Sabine L.
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 4(2016)
• Page Start: 1511
• Page End: 1513
• Publication Date: 2015-12-21
• Subjects: aminations -- biocatalysis -- chiral amines -- enzyme cascades -- whole-cell biotransformation; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201510028
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: Enantiomerically pure chiral amines are ubiquitous chemical building blocks in bioactive pharmaceutical products and their synthesis from simple starting materials is of great interest. One of the most attractive strategies is the stereoselective installation of a chiral amine through C−H amination, which is a challenging chemical transformation. Herein we report the application of a multienzyme cascade, generated in a single bacterial whole‐cell system, which is able to catalyze stereoselective benzylic aminations with ee values of 97.5 %. The cascade uses four heterologously expressed recombinant enzymes with cofactors provided by the host cell and isopropyl amine added as the amine donor. The cascade presents the first example of the successful de novo design of a single whole‐cell biocatalyst for formal stereoselective C−H amination. Abstract : Enantiomerically pure chiral amines are ubiquitous chemical building blocks in bioactive pharmaceuticals and their synthesis from simple starting materials is of great interest. One strategy is the stereoselective installation of a chiral amine through formal C−H amination. A multienzyme cascade was constructed and applied in a single bacterial whole cell that can catalyze stereoselective benzylic aminations with 97.5 % ee .