Lipase-catalyzed dynamic kinetic resolution of dimethyl (1,3-dihydro-2H-isoindol-1-yl)phosphonate

A simple dynamic kinetic resolution of dimethyl (1,3-dihydro-2H-isoindol-1-yl)phosphonate has been developed by means of a lipase-catalyzed alkoxycarbonylation reaction. The influence of reaction parameters such as solvent, type and amount of alkoxycarbonylating agent, source and loading of enzyme,...

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Bibliographic Details
Published in:Tetrahedron
Main Authors: Arizpe, Alicia, Sayago, Francisco J., Gotor, Vicente, Cativiela, Carlos, Gotor-Fernández, Vicente
Other Authors: Gobierno de Aragón, European Commission, Ministerio de Economía y Competitividad (España), Consejo Superior de Investigaciones Científicas (España), Fundación para el Fomento en Asturias de la Investigación Científica Aplicada y la Tecnología, Principado de Asturias
Format: Article in Journal/Newspaper
Language:unknown
Published: Elsevier 2016
Subjects:
Enzymes
Dynamic kinetic resolution
Asymmetric synthesis
Aminophosphonates
Isoindoline
Antarc*
Antarctica
Online Access:http://hdl.handle.net/10261/154902
https://doi.org/10.1016/j.tet.2016.02.015
https://doi.org/10.13039/501100000780
https://doi.org/10.13039/501100003329
https://doi.org/10.13039/501100003339
https://doi.org/10.13039/501100008430
https://doi.org/10.13039/501100010067
https://doi.org/10.13039/100011941
Description
Summary:A simple dynamic kinetic resolution of dimethyl (1,3-dihydro-2H-isoindol-1-yl)phosphonate has been developed by means of a lipase-catalyzed alkoxycarbonylation reaction. The influence of reaction parameters such as solvent, type and amount of alkoxycarbonylating agent, source and loading of enzyme, substrate concentration, temperature, and reaction time has been studied. The best results were found in the biocatalyzed reaction using Candida antarctica lipase type A and allyl 3-methoxyphenyl carbonate in toluene at 30 °C, yielding the (R)-allyl carbamate in 58% isolated yield and 96% enantiomeric excess. Remarkably, this procedure does not require external auxiliaries for the racemization of the slow-reacting aminophosphonate enantiomer and occurs under mild reaction conditions. Financial support to this work was provided by Ministerio de Economía y Competitividad-FEDER (grants CTQ2013-44153-P, and CTQ2013-40855-R), Gobierno de Aragón-Fondo Social Europeo (research group E40) and Gobierno del Principado de Asturias (FC-15-GRUPIN14-002). M.L.-I. thanks FICYT for a predoctoral fellowship. A.A. thanks the Spanish Consejo Superior de Investigaciones Científicas for a JAE predoctoral fellowship. Peer Reviewed

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