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Enzymatic Late‐Stage Modifications: Better Late Than Never
Author(s) -
Romero Elvira,
Jones Bethan S.,
Hogg Bethany N.,
Rué Casamajo Arnau,
Hayes Martin A.,
Flitsch Sabine L.,
Turner Nicholas J.,
Schnepel Christian
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202014931
Subject(s) - biocatalysis , enzyme , chemistry , biochemical engineering , combinatorial chemistry , amide , computational biology , nanotechnology , catalysis , biochemistry , biology , materials science , engineering , reaction mechanism
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.