Enzyme-catalyzed kinetic resolution of N-Boc-trans-3-hydroxy-4-phenylpyrrolidine

• Published in: Central European journal of chemistry Vol. 12; no. 1; pp. 25 - 32
• Main Authors: Faigl, Ferenc, Kovács, Ervin, Balogh, Dóra, Holczbauer, Tamás, Czugler, Mátyás, Simándi, Béla
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 2014; Versita; De Gruyter
• Subjects: 3-hydroxy-4-phenylpyrrolidine; Biochemistry; Biological and Medical Physics; Biophysics; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Enantioselective alcoholysis; Enzymatic hydrolysis; Enzyme-catalyzed resolution; Geochemistry; Lipase enzymes; Research Article; Lipase enzymes; Enantioselective alcoholysis; Enzyme-catalyzed resolution; 3-hydroxy-4-phenylpyrrolidine; Enzymatic hydrolysis
• ISSN: 1895-1066; 2391-5420; 1644-3624; 2391-5420
• DOI: 10.2478/s11532-013-0347-8

The first enzyme-catalyzed kinetic resolution of tert -butyl-3-hydroxy-4-phenylpyrrolidine-1-carboxylate is presented. Enzyme, solvent and temperature optimization resulted in a new resolution method with E = 40 enantioselectivity. The acetate derivative of the (+)-(3 S ,4 R ) enantiomer formed while the (−)-(3R,4S) isomer remained intact. Very good enantioselectivities (E > 200) were achieved in the enzyme-catalyzed alcoholysis of the racemic acetate in i -propanol and t -butanol where the (+)-(3 S ,4 R ) enantiomer was prepared in pure form (ee > 99.7%). Absolute configuration of the (−)-(3 R ,4 S )-enantiomer was determined by single crystal X-ray diffraction method.