Highly enantioselective enzymatic resolution of aromatic beta-amino acid amides with Pd-catalyzed racemization

• Published in: Tetrahedron: Asymmetry
• Main Authors: Choi, E, Kim, Y, Ahn, Y, Park, J, Kim, MJ
• Other Authors: 화학과, 10052207
• Format: Article in Journal/Newspaper
• Language: English
• Published: PERGAMON-ELSEVIER SCIENCE LTD 2013
• Subjects: DYNAMIC KINETIC RESOLUTION; CANDIDA-ANTARCTICA LIPASE; ALCOHOL REACTS FASTER; ACTIVE-SITE MODEL; PSEUDOMONAS-STUTZERI LIPASE; SECONDARY ALCOHOLS; ASYMMETRIC-SYNTHESIS; ACYLATION; ENANTIOMERS; ESTERS; DERIVATIVES; HYDROLYSIS; Antarc*; Antarctica
• Online Access: https://oasis.postech.ac.kr/handle/2014.oak/14067; https://doi.org/10.1016/J.TETASY.2013.09.022

The kinetic resolution of an aromatic beta-amino acid amide 3a-d via N-acylation was explored with two lipases, Candida antarctica lipase A (CALA) and Pseudomonas stutzeri lipase (PSL). The PSL-catalyzed resolution proceeded with excellent enantioselectivity (E = >400) to give both acylated products and unreacted substrates in enantiopure forms. Three additional aromatic beta-amino acid amides 3b-d were also resolved by PSL with a high level of enantioselectivity (E = >200). The PSL-catalyzed resolution of 3a was coupled with a Pd-catalyzed racemization to obtain enantiopure N-acylated product (R)-4a (>99% ee) in high yield (90%). (C) 2013 Elsevier Ltd. All rights reserved. X 1 1 7 9 scie scopus