Chemoenzymatic dynamic kinetic resolution of primary amines.
An efficient process for dynamic kinetic resolution of amines was developed by combining a ruthenium-catalyzed racemization with a lipase-catalyzed resolution. A variety of unfunctionalized primary amines were transformed into one enantiomer of the amide in high yield and high enantioselectivity.
Paetzold
Jens
J
Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, SE-10691 Stockholm, Sweden.
Bäckvall
Jan E
JE
D000588:Amines / Q000737:chemistry / Q000302:isolation & purification*; D002384:Catalysis; D005656:Fungal Proteins; D007097:Imines / Q000737:chemistry; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism; D013237:Stereoisomerism
D000588:Amines; D005656:Fungal Proteins; D007097:Imines; D008049:Lipase; C431349:lipase B, Candida antarctica