title: Enzymatic resolution of bicyclic 1-heteroarylamines using Candida antarctica lipase B.
abstract: Candida antarctica lipase B has been used to kinetically resolve a structurally diverse series of bicyclic 1-heteroaryl primary amines by enantioselective acetylation. High yields of either enantiomer could be obtained with excellent enantioselectivity (90-99% ee), while the undesired enantiomer could, in some cases, be recycled by thermal racemization. The absolute stereochemistry of the products was confirmed by an X-ray crystal structure.
authors.affiliation: AnorMED Inc., #200-20353 64th Avenue, Langley, BC, Canada V2Y 1N5.
authors.forename: Krystyna A
authors.initials: KA
authors.lastname: Skupinska
authors.forename: Ernest J
authors.initials: EJ
authors.lastname: McEachern
authors.forename: Ian R
authors.initials: IR
authors.lastname: Baird
authors.forename: Renato T
authors.initials: RT
authors.lastname: Skerlj
authors.forename: Gary J
authors.initials: GJ
authors.lastname: Bridger
mesh_terms: D000107:Acetylation; D000588:Amines / Q000032:analysis / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D018360:Crystallography, X-Ray; D005656:Fungal Proteins; D007202:Indicators and Reagents; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008968:Molecular Conformation; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D013237:Stereoisomerism
chemical_list: D000588:Amines; D005656:Fungal Proteins; D007202:Indicators and Reagents; D008049:Lipase; C431349:lipase B, Candida antarctica