Premium
Synthesis of Optically Active Amines Employing Recombinant ω‐Transaminases in E. coli Cells
Author(s) -
Koszelewski Dominik,
Göritzer Madeleine,
Clay Dorina,
Seisser Birgit,
Kroutil Wolfgang
Publication year - 2010
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.200900220
Subject(s) - kinetic resolution , reductive amination , amination , transaminase , chemistry , stereoselectivity , enantiomeric excess , enantiomer , yield (engineering) , catalysis , amine gas treating , combinatorial chemistry , enantioselective synthesis , organic chemistry , enzyme , materials science , metallurgy
Various recombinant ω‐transaminases, overexpressed in E. coli cells and employed as whole‐cell catalysts, are tested for the synthesis of enantiomerically pure amines from the corresponding prochiral ketones. Optically pure ( S )‐amines are obtained by formal reductive amination, consuming just ammonia and a cheap reducing agent (formate) with up to 99 % ee and 97 % yield. The other enantiomer was accessible by employing the same ω‐transaminases in a kinetic resolution starting from racemic amines. A ω‐transaminase derived from an Arthrobacter species displayed the highest stereoselectivity for all substrates tested, both for the kinetic resolution of rac ‐amines and for the amination of ketones.