Enzymatic resolution of bicyclic 1-heteroarylamines using Candida antarctica lipase B.
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.
Skupinska
Krystyna A
KA
AnorMED Inc., #200-20353 64th Avenue, Langley, BC, Canada V2Y 1N5.
McEachern
Ernest J
EJ
Baird
Ian R
IR
Skerlj
Renato T
RT
Bridger
Gary J
GJ
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
D000588:Amines; D005656:Fungal Proteins; D007202:Indicators and Reagents; D008049:Lipase; C431349:lipase B, Candida antarctica