Promiscuous activity of C-acyltransferase from Pseudomonas protegens: synthesis of acetanilides in aqueous buffer
| Autor: | Wolfgang Kroutil, Nina G. Schmidt, Anna Żądło-Dobrowolska |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
biology
010405 organic chemistry Phenyl acetate Stereochemistry education Metals and Alloys General Chemistry 010402 general chemistry biology.organism_classification 01 natural sciences Chemical synthesis Catalysis 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials chemistry.chemical_compound Pseudomonas protegens Aniline chemistry Biocatalysis Amide Acyltransferase Materials Chemistry Ceramics and Composites Peptide bond |
| Zdroj: | Chemical Communications. 54:3387-3390 |
| ISSN: | 1364-548X 1359-7345 |
| DOI: | 10.1039/c8cc00290h |
| Popis: | Amide bond formation has considerable significance in synthetic chemistry. Although the C-acyltransferase from Pseudomonas protegens has been found to catalyze C-C bond formation in nature as well as in in vitro experiments with non-natural substrates, it is now shown that the enzyme is also able to catalyze amide formation using aniline derivatives as substrates with promiscuous activity. Importantly, the amide formation was enabled in aqueous buffer. Identifying phenyl acetate as the most suitable acetyl donor, the products were obtained with up to >99% conversion and up to 99% isolated yield. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|