Highly enantioselective enzymatic resolution of aromatic beta-amino acid amides with Pd-catalyzed racemization
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 produ...
Published in: | Tetrahedron: Asymmetry |
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Main Authors: | , , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
PERGAMON-ELSEVIER SCIENCE LTD
2013
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Subjects: | |
Online Access: | https://oasis.postech.ac.kr/handle/2014.oak/14067 https://doi.org/10.1016/J.TETASY.2013.09.022 |
Summary: | 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 |
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