Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1H NMR reveals fine details of substrate specificity
- Resource Type
- Authors
- Silvia De Cesare; Juraj Bella; Lorna Murray; Nicholas Phillip Mulholland; Catherine A McKenna; Dominic J. Campopiano
- Source
- De Cesare, S, Mckenna, C A, Mulholland, N, Murray, L, Bella, J & Campopiano, D J 2021, ' Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1 H NMR reveals fine details of substrate specificity ', Organic & Biomolecular chemistry . https://doi.org/10.1039/D1OB00122A
- Subject
- chemistry.chemical_classification
010405 organic chemistry
Chemistry
Organic Chemistry
Substrate (chemistry)
010402 general chemistry
01 natural sciences
Biochemistry
Combinatorial chemistry
0104 chemical sciences
Amino acid
Hydrolysis
Enantiopure drug
Acetylation
Biocatalysis
Proton NMR
Physical and Theoretical Chemistry
Selectivity
- Language
- English
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.