ArticleAngewandte Chemie (International ed. in English)2022
Transesterification of Non-Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Synthetic Mimics of Serine Proteases via Covalent Imprinting of Photo-Protected Template Molecules for Aryl Amide Hydrolysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Turning Enzyme Models into Model Enzymes in a Substrate-Tailored, Desolvated Active Site.ACS catalysis · 2025Article
- Efficient Cleavage of pUC19 DNA by Tetraaminonaphthols.ChemistryOpen · 2025Article
- Transesterification of Non-Activated Esters Promoted by Small Molecules Mimicking the Active Site of Hydrolases.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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