Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis
A series of hydroxy-, methoxy-, and nitrophenylacetamides was synthesized by enzyme catalysis. The 28 new products were obtained through a lipase-catalyzed two-step reaction in very good to excellent yield. In the case of nitro derivatives, a one-pot, two-step methodology allowed the desired product...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_1434193X_v2014_n29_p6439_GarciaLinares |
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todo:paper_1434193X_v2014_n29_p6439_GarciaLinares2023-10-03T16:14:13Z Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis García Liñares, G. Arroyo Mañez, P. Baldessari, A. Amides Enzyme catalysis Esters Molecular modeling Reaction mechanisms A series of hydroxy-, methoxy-, and nitrophenylacetamides was synthesized by enzyme catalysis. The 28 new products were obtained through a lipase-catalyzed two-step reaction in very good to excellent yield. In the case of nitro derivatives, a one-pot, two-step methodology allowed the desired products to be obtained in high yields. The influence of various reaction parameters in the lipase-catalyzed reactions, such as enzyme source, nucleophile (alcohol or amine)/substrate ratio, enzyme/substrate ratio, solvent and temperature were studied. It was observed that nitro-substituted phenylacetates were more reactive in the aminolysis reaction than phenylacetates substituted with a hydroxyl group. To study this substituent effect, a Hammett analysis and the determination of the ρ parameter were carried out. Moreover, a computational study was applied to the most representative systems, performing an exploration of the potential energy surface for the catalyzed and noncatalyzed aminolysis reaction for nitro- and hydroxyphenylacetates. Both analysis showed that the presence of a strongly electron-attracting group favors the activity of the enzyme, in complete agreement with the experimental results of the enzymatic catalysis. © 2014 Wiley-VCH Verlag GmbH & Co. KGaA. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_1434193X_v2014_n29_p6439_GarciaLinares |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Amides Enzyme catalysis Esters Molecular modeling Reaction mechanisms |
| spellingShingle |
Amides Enzyme catalysis Esters Molecular modeling Reaction mechanisms García Liñares, G. Arroyo Mañez, P. Baldessari, A. Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| topic_facet |
Amides Enzyme catalysis Esters Molecular modeling Reaction mechanisms |
| description |
A series of hydroxy-, methoxy-, and nitrophenylacetamides was synthesized by enzyme catalysis. The 28 new products were obtained through a lipase-catalyzed two-step reaction in very good to excellent yield. In the case of nitro derivatives, a one-pot, two-step methodology allowed the desired products to be obtained in high yields. The influence of various reaction parameters in the lipase-catalyzed reactions, such as enzyme source, nucleophile (alcohol or amine)/substrate ratio, enzyme/substrate ratio, solvent and temperature were studied. It was observed that nitro-substituted phenylacetates were more reactive in the aminolysis reaction than phenylacetates substituted with a hydroxyl group. To study this substituent effect, a Hammett analysis and the determination of the ρ parameter were carried out. Moreover, a computational study was applied to the most representative systems, performing an exploration of the potential energy surface for the catalyzed and noncatalyzed aminolysis reaction for nitro- and hydroxyphenylacetates. Both analysis showed that the presence of a strongly electron-attracting group favors the activity of the enzyme, in complete agreement with the experimental results of the enzymatic catalysis. © 2014 Wiley-VCH Verlag GmbH & Co. KGaA. |
| format |
JOUR |
| author |
García Liñares, G. Arroyo Mañez, P. Baldessari, A. |
| author_facet |
García Liñares, G. Arroyo Mañez, P. Baldessari, A. |
| author_sort |
García Liñares, G. |
| title |
Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| title_short |
Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| title_full |
Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| title_fullStr |
Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| title_full_unstemmed |
Lipase-catalyzed synthesis of substituted phenylacetamides: Hammett analysis and computational study of the enzymatic aminolysis |
| title_sort |
lipase-catalyzed synthesis of substituted phenylacetamides: hammett analysis and computational study of the enzymatic aminolysis |
| url |
http://hdl.handle.net/20.500.12110/paper_1434193X_v2014_n29_p6439_GarciaLinares |
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