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Enzymatic Racemization of Amines Catalyzed by Enantiocomplementary ω‐Transaminases
Author(s) -
Koszelewski Dominik,
Grischek Barbara,
Glueck Silvia M.,
Kroutil Wolfgang,
Faber Kurt
Publication year - 2011
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201001602
Subject(s) - racemization , transamination , chemistry , amine gas treating , enantiomer , catalysis , biocatalysis , enantiomeric excess , enzyme , ketone , stereoselectivity , organic chemistry , combinatorial chemistry , stereochemistry , enantioselective synthesis , reaction mechanism
A strategy for the biocatalytic racemization of primary α‐chiral amines was developed by employing a pair of stereocomplementary PLP‐dependent ω‐transaminases. The interconversion of amine enantiomers proceeded through reversible transamination by a prochiral ketone intermediate, either catalyzed by a pair of stereocomplementary ω‐transaminases or by a single enzyme possessing low stereoselectivity. To tune the system, the type and concentration of a nonchiral amino acceptor proved to be crucial. Finally, racemization could be achieved by the cross‐transamination of two different amines without a requirement for an external amino acceptor. Several synthetically and industrially important amines could be enzymatically racemized under mild reaction conditions.