The N-Acetyl Amino Acid Racemases (NAAARs); Native and evolved biocatalysts applied to the synthesis of canonical and non-canonical amino acids.

Silvia De Cesare, Dominic J Campopiano

Journal: Current opinion in biotechnology 2021;69():212-220

PMID: 33556834

Abstract

Amino acids are one of the most important synthons employed in the biotechnology, pharmaceutical and agrochemical industries for the preparation of active agents. Recently, the emerging use of these compounds as tools for protein engineering, has also been reported. Numerous chemo- and biocatalytic strategies have been developed for the stereoselective synthesis of these compounds. One of the most efficient processes is the enzymatic dynamic kinetic resolution of N-acylated derivatives, where an N-acyl amino acid racemase (NAAAR) is coupled with an enantioselective, hydrolytic enzyme (aminoacylase), and used to convert a racemic mixture of starting materials to enantiopure products. Here we provide a brief overview of the structure and mechanism of NAAAR. We will also review the applications of this class of biocatalyst, as well as discussing the various strategies employed to obtain an efficient system for the synthesis of optically pure canonical and non-canonical amino acids.

Copyright © 2021 Elsevier Ltd. All rights reserved.

Address: EaStChem School of Chemistry, University of Edinburgh, David Brewster Road, King's Buildings, Edinburgh, EH9 3FJ, UK.; EaStChem School of Chemistry, University of Edinburgh, David Brewster Road, King's Buildings, Edinburgh, EH9 3FJ, UK. Electronic address: [email protected].

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