Enzymatic Late‐Stage Modifications: Better Late Than Never

Romero, Elvira; Jones, Bethan S.; Hogg, Bethany N.; Rué Casamajo, Arnau; Hayes, Martin A.; Flitsch, Sabine L.; Turner, Nicholas J.; Schnepel, Christian

Abstract

Enzyme catalysis is gaining increasing importance in synthetic chemistry. Nowadays, the growing number of biocatalysts accessible by means of bioinformatics and enzyme engineering opens up an immense variety of selective reactions. Biocatalysis especially provides excellent opportunities for late-stage modification often superior to conventional de novo synthesis. Enzymes have proven to be useful for direct introduction of functional groups into complex scaffolds, as well as for rapid diversification of compound libraries. Particularly important and highly topical are enzyme-catalysed oxyfunctionalisations, halogenations, methylations, reductions, and amide bond formations due to the high prevalence of these motifs in pharmaceuticals. This Review gives an overview of the strengths and limitations of enzymatic late-stage modifications using native and engineered enzymes in synthesis while focusing on important examples in drug development.

Citation

Romero, E., Jones, B. S., Hogg, B. N., Rué Casamajo, A., Hayes, M. A., Flitsch, S. L., Turner, N. J., & Schnepel, C. (2021). Enzymatic Late‐Stage Modifications: Better Late Than Never. Angewandte Chemie International Edition, 60(31), 16824-16855. https://doi.org/10.1002/anie.202014931

• Journal Article Type: Article
• Acceptance Date: Jan 16, 2021
• Online Publication Date: Mar 8, 2021
• Publication Date: Jul 26, 2021
• Deposit Date: Jan 1, 2025
• Journal: Angewandte Chemie International Edition
• Print ISSN: 1433-7851
• Electronic ISSN: 1521-3773
• Publisher: Wiley
• Peer Reviewed: Peer Reviewed
• Volume: 60
• Issue: 31
• Pages: 16824-16855
• DOI: https://doi.org/10.1002/anie.202014931
• Public URL: https://durham-repository.worktribe.com/output/3263725