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...

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Bibliographic Details
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
Description
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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