Issue 27, 2018

Promiscuous activity of C-acyltransferase from Pseudomonas protegens: synthesis of acetanilides in aqueous buffer

Abstract

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.

Graphical abstract: Promiscuous activity of C-acyltransferase from Pseudomonas protegens: synthesis of acetanilides in aqueous buffer

Supplementary files

Article information

Article type
Communication
Submitted
17 Jan 2018
Accepted
08 Mar 2018
First published
19 Mar 2018
This article is Open Access
Creative Commons BY license

Chem. Commun., 2018,54, 3387-3390

Promiscuous activity of C-acyltransferase from Pseudomonas protegens: synthesis of acetanilides in aqueous buffer

A. Żądło-Dobrowolska, N. G. Schmidt and W. Kroutil, Chem. Commun., 2018, 54, 3387 DOI: 10.1039/C8CC00290H

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