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Issue 22, 2021

Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1H NMR reveals fine details of substrate specificity

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Abstract

Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that the L-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range of N-acyl-amino acid substrates. This activity was revealed by 1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.

Graphical abstract: Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1H NMR reveals fine details of substrate specificity

Supplementary files

Article information


Submitted
22 Jan 2021
Accepted
30 Apr 2021
First published
03 May 2021

This article is Open Access

Org. Biomol. Chem., 2021,19, 4904-4909
Article type
Paper

Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1H NMR reveals fine details of substrate specificity

S. De Cesare, C. A. McKenna, N. Mulholland, L. Murray, J. Bella and D. J. Campopiano, Org. Biomol. Chem., 2021, 19, 4904 DOI: 10.1039/D1OB00122A

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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