Both Enantiomers of N-Boc-indoline-2-carboxylic Esters
Abstract An immobilized form of Candida antarctica lipase (Chirazyme L-2) catalyzed enantioselective hydrolysis (E > 1000) of N-Boc-indoline-2-carboxylic acid methyl ester. The reaction proceeded efficiently at 60 °C, a temperature over the melting point of substrate, in the conversion of 49....
| Published in: | Bulletin of the Chemical Society of Japan |
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| Main Authors: | , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Oxford University Press (OUP)
2004
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1246/bcsj.77.1021 https://academic.oup.com/bcsj/article-pdf/77/5/1021/56264213/bcsj.77.1021.pdf |
| Summary: | Abstract An immobilized form of Candida antarctica lipase (Chirazyme L-2) catalyzed enantioselective hydrolysis (E > 1000) of N-Boc-indoline-2-carboxylic acid methyl ester. The reaction proceeded efficiently at 60 °C, a temperature over the melting point of substrate, in the conversion of 49.9% to provide the hydrolyzed product, (S)-carboxylic acid with >99.9% ee and the unreacted (R)-ester with 99.6% ee. A newly developed expeditious route to the racemic substrate (a total of six steps, 60% yield), starting from aniline and ethyl α-methylacetoacetate, established the scalable chemo-enzymatic synthesis of the desired compounds in both enantiomerically pure forms. |
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