Enzymatic Resolution of Bicyclic 1-Heteroarylamines Using Candida antarctica Lipase B

• Published in: Journal of organic chemistry Vol. 68; no. 9; pp. 3546 - 3551
• Main Authors: Skupinska, Krystyna A., McEachern, Ernest J., Baird, Ian R., Skerlj, Renato T., Bridger, Gary J.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 02.05.2003
• Subjects: Acetylation; Amines - analysis; Amines - chemistry; Amines - metabolism; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Catalysis; Crystallography, X-Ray; Fundamental and applied biological sciences. Psychology; Fungal Proteins; Indicators and Reagents; Kinetics; Lipase - metabolism; Methods. Procedures. Technologies; Molecular Conformation; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Stereoisomerism; Separation; Enantioselectivity; Molecular structure; Enzyme; Racemization; Triacylglycerol lipase; Esterases; X ray diffraction; Carboxylic ester hydrolases; Enzymatic method; Amine; Optical resolution; Hydrolases; Acetylation; Heterocyclic compound
• ISSN: 0022-3263; 1520-6904
• DOI: 10.1021/jo026701r

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.