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Full Paper
Promiscuous Behavior of Rhizomucor miehei Lipase in the Synthesis of N-Substituted β-Amino Esters
Article first published online: 27 DEC 2011
DOI: 10.1002/ejoc.201101624
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Monsalve, L. N., Gillanders, F. and Baldessari, A. (2012), Promiscuous Behavior of Rhizomucor miehei Lipase in the Synthesis of N-Substituted β-Amino Esters. Eur. J. Org. Chem., 2012: 1164–1170. doi: 10.1002/ejoc.201101624
Publication History
- Issue published online: 13 FEB 2012
- Article first published online: 27 DEC 2011
- Manuscript Received: 10 NOV 2011
Funded by
- Universidad de Buenos Aires (UBA). Grant Number: (X010)
- Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Grant Number: PIP 112-200801-00801/09
- Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT). Grant Number: (PICT 2005-32735
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Keywords:
- Enzyme catalysis;
- Amino esters;
- Michael addition
Abstract
A mild and efficient procedure for the aza-Michael addition of amines to acrylates by using lipases as catalysts is reported. Various lipases, mono- and bifunctional amines, alkyl acrylates, and reaction parameters were studied. Under the optimal conditions, Rhizomucor miehei lipase showed high selectivity. It catalyzed the formation of the Michael monoadduct as the only product in high yield and purity. Moreover, when diamines were used as nucleophiles, the lipase catalyzed the addition of only one of the two amino groups, showing in this case high substrate specificity. This promiscuous and highly selective behavior displayed by Rhizomucor miehei lipase allowed us to obtain 22 N-substituted β-amino esters, 15 of them being new products.