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, a transformation which is
chemically challenging. Herein we report the application of a
multienzyme cascade, generated in a single bacterial whole cell
system, which is able to catalyse 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
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, a transformation which is
chemically challenging. Herein we report the application of a
multienzyme cascade, generated in a single bacterial whole cell
system, which is able to catalyse 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
| Original language | English |
|---|---|
| Journal | Angewandte Chemie (International Edition) |
| Early online date | 21 Dec 2015 |
| DOIs | |
| Publication status | Published - 18 Jan 2016 |