title: Enzymatic racemization of amines catalyzed by enantiocomplementary ω-transaminases.
abstract: 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.
authors.affiliation: Austrian Centre of Industrial Biotechnology (ACIB) c/o, Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010 Graz, Austria.
authors.forename: Dominik
authors.initials: D
authors.lastname: Koszelewski
authors.forename: Barbara
authors.initials: B
authors.lastname: Grischek
authors.forename: Silvia M
authors.initials: SM
authors.lastname: Glueck
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Kroutil
authors.forename: Kurt
authors.initials: K
authors.lastname: Faber
mesh_terms: D000588:Amines / Q000737:chemistry* / Q000378:metabolism; D001410:Bacillus megaterium / Q000201:enzymology; D002384:Catalysis; D002861:Chromobacterium / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D007659:Ketones / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D013237:Stereoisomerism; D000637:Transaminases / Q000737:chemistry / Q000378:metabolism*; D014733:Vibrio / Q000201:enzymology
chemical_list: D000588:Amines; D007659:Ketones; D000637:Transaminases