Kinetic Resolution of Nearly Symmetric 3‑Cyclohexene-1-carboxylate Esters Using a Bacterial Carboxylesterase Identified by Genome Mining

A new bacterial carboxylesterase (CarEst3) was identified by genome mining and found to efficiently hydrolyze racemic methyl 3-cyclohexene-1-carboxylate (rac-CHCM) with a nearly symmetric structure for the synthesis of (S)-CHCM. CarEst3 displayed a high substrate tolerance and a stable catalytic per...

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Bibliographic Details
Published inOrganic letters Vol. 23; no. 8; pp. 3043 - 3047
Main Authors Dou, Zhe, Chen, Xuanzao, Niwayama, Satomi, Xu, Guochao, Ni, Ye
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 16.04.2021
Amer Chemical Soc
Subjects
Chemistry
Chemistry, Organic
Physical Sciences
Science & Technology
ASYMMETRIC-SYNTHESIS
PHEROMONE SYNTHESIS
ENZYMES
CONVERGENT
FRAGMENT
FK-506
STEREOSELECTIVE-SYNTHESIS
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Summary:A new bacterial carboxylesterase (CarEst3) was identified by genome mining and found to efficiently hydrolyze racemic methyl 3-cyclohexene-1-carboxylate (rac-CHCM) with a nearly symmetric structure for the synthesis of (S)-CHCM. CarEst3 displayed a high substrate tolerance and a stable catalytic performance. The enantioselective hydrolysis of 4.0 M (560 g·L–1) rac-CHCM was accomplished, yielding (S)-CHCM with a >99% ee, a substrate to catalyst ratio of 1400 g·g–1, and a space-time yield of 538 g·L–1·d–1.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.1c00714