title: Chemoenzymatic dynamic kinetic resolution of primary amines.
abstract: 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.
authors.affiliation: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, SE-10691 Stockholm, Sweden.
authors.forename: Jens
authors.initials: J
authors.lastname: Paetzold
authors.forename: Jan E
authors.initials: JE
authors.lastname: Bäckvall
mesh_terms: 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
chemical_list: D000588:Amines; D005656:Fungal Proteins; D007097:Imines; D008049:Lipase; C431349:lipase B, Candida antarctica