Petchey, Mark and Grogan, Gideon James orcid.org/0000-0003-1383-7056 (2019) Enzyme-catalyzed Synthesis of Secondary and Tertiary Amides. Advanced Synthesis and Catalysis. pp. 3895-3914. ISSN 1615-4150
Abstract
Abstract The synthesis of the amide bond between an amine and a carboxylic acid is one of the most significant reactions in industrial pharmaceutical synthesis. Despite the apparent simplicity of synthetic methods for amide bond formation, many of these are disadvantaged by their requirement for toxic or hazardous reagents for the activation of the acid component, or poor atom economy resulting from the need for stoichiometric amounts of coupling reagents. In this context, biocatalysis has emerged as an alternative catalytic method for amide bond formation, presenting the advantages of both environmentally benign reagents and conditions and also atom economy. In this review we detail developments in the enzyme-catalyzed preparation of secondary and tertiary amides for the synthesis of pharmaceutical-type molecules and review the applications of hydrolases, such as lipases and penicillin acylases, to these reactions. We also summarise the activity of ATP-dependent enzymes for amide bond formation and assess their potential for the preparative synthesis of amides from carboxylic acids and amines in aqueous media. Keywords: Biocatalysis, Amides, Lipase, Penicillin Acylase, NRPS, Amide Bond Synthetase
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Dates: |
|
Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 29 Aug 2019 08:30 |
Last Modified: | 08 Feb 2025 00:34 |
Published Version: | https://doi.org/10.1002/adsc.201900694 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1002/adsc.201900694 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:150173 |