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Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases

The synthesis of small molecules able to mimic the active site of hydrolytic enzymes has been largely pursued in recent decades. The high reaction rates and specificity shown by natural hydrolases present an attractive target, and yet the preparation of suitable small‐molecule mimics remains challen...

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Autores principales: Garrido‐González, José J., Sánchez‐Santos, Estela, Habib, Asmaa, Cuevas Ferreras, Ángel V., Sanz, Francisca, Morán, Joaquín R., Fuentes de Arriba, Ángel L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9544131/
https://www.ncbi.nlm.nih.gov/pubmed/35580193
http://dx.doi.org/10.1002/anie.202206072
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author Garrido‐González, José J.
Sánchez‐Santos, Estela
Habib, Asmaa
Cuevas Ferreras, Ángel V.
Sanz, Francisca
Morán, Joaquín R.
Fuentes de Arriba, Ángel L.
author_facet Garrido‐González, José J.
Sánchez‐Santos, Estela
Habib, Asmaa
Cuevas Ferreras, Ángel V.
Sanz, Francisca
Morán, Joaquín R.
Fuentes de Arriba, Ángel L.
author_sort Garrido‐González, José J.
collection PubMed
description The synthesis of small molecules able to mimic the active site of hydrolytic enzymes has been largely pursued in recent decades. The high reaction rates and specificity shown by natural hydrolases present an attractive target, and yet the preparation of suitable small‐molecule mimics remains challenging, requiring activated substrates to achieve productive outcomes. Here we present small synthetic artificial enzymes which mimic the catalytic site and the oxyanion hole of chymotrypsin and N‐terminal hydrolases and are able to perform, for the first time, the transesterification of a non‐activated ester such as ethyl acetate with methanol under mild and neutral reaction conditions.
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spelling pubmed-95441312022-10-14 Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases Garrido‐González, José J. Sánchez‐Santos, Estela Habib, Asmaa Cuevas Ferreras, Ángel V. Sanz, Francisca Morán, Joaquín R. Fuentes de Arriba, Ángel L. Angew Chem Int Ed Engl Research Articles The synthesis of small molecules able to mimic the active site of hydrolytic enzymes has been largely pursued in recent decades. The high reaction rates and specificity shown by natural hydrolases present an attractive target, and yet the preparation of suitable small‐molecule mimics remains challenging, requiring activated substrates to achieve productive outcomes. Here we present small synthetic artificial enzymes which mimic the catalytic site and the oxyanion hole of chymotrypsin and N‐terminal hydrolases and are able to perform, for the first time, the transesterification of a non‐activated ester such as ethyl acetate with methanol under mild and neutral reaction conditions. John Wiley and Sons Inc. 2022-06-07 2022-08-26 /pmc/articles/PMC9544131/ /pubmed/35580193 http://dx.doi.org/10.1002/anie.202206072 Text en © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Research Articles
Garrido‐González, José J.
Sánchez‐Santos, Estela
Habib, Asmaa
Cuevas Ferreras, Ángel V.
Sanz, Francisca
Morán, Joaquín R.
Fuentes de Arriba, Ángel L.
Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title_full Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title_fullStr Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title_full_unstemmed Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title_short Transesterification of Non‐Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases
title_sort transesterification of non‐activated esters promoted by small molecules mimicking the active site of hydrolases
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9544131/
https://www.ncbi.nlm.nih.gov/pubmed/35580193
http://dx.doi.org/10.1002/anie.202206072
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