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

Silvia De Cesare; Catherine A. Mckenna; Nicholas Mulholland; Lorna Murray; Juraj Bella; Dominic J. Campopiano

doi:10.1039/D1OB00122A

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

Silvia De Cesare, Catherine A. Mckenna, Nicholas Mulholland, Lorna Murray, Juraj Bella, Dominic J. Campopiano

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Number of pages	6
Journal	Organic & Biomolecular chemistry
Early online date	3 May 2021
DOIs	https://doi.org/10.1039/D1OB00122A
Publication status	E-pub ahead of print - 3 May 2021

Access to Document

10.1039/D1OB00122A

20210520_Campopiano_d1ob00122aFinal published version, 601 KBLicence: Creative Commons: Attribution (CC-BY)

http://xlink.rsc.org/?DOI=D1OB00122ALicence: Creative Commons: Attribution (CC-BY)

Fingerprint Dive into the research topics of 'Direct monitoring of biocatalytic deacetylation of amino acid substrates by <sup>1</sup>H NMR reveals fine details of substrate specificity'. Together they form a unique fingerprint.

1 Finished

A National Network for Applications of High-Field NMR in the Life and Physical Sciences
Uhrin, D., Barlow, P., Bell, N. & Bramham, J.
EPSRC
1/05/18 → 30/04/21
Project: Research

Cite this

@article{8488592544a24cb695dd638401071ea8,

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

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.",

author = "{De Cesare}, Silvia and Mckenna, {Catherine A.} and Nicholas Mulholland and Lorna Murray and Juraj Bella and Campopiano, {Dominic J.}",

year = "2021",

month = may,

day = "3",

doi = "10.1039/D1OB00122A",

language = "English",

journal = "Organic & Biomolecular chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

}

TY - JOUR

T1 - Direct monitoring of biocatalytic deacetylation of amino acid substrates by 1H NMR reveals fine details of substrate specificity

AU - De Cesare, Silvia

AU - Mckenna, Catherine A.

AU - Mulholland, Nicholas

AU - Murray, Lorna

AU - Bella, Juraj

AU - Campopiano, Dominic J.

PY - 2021/5/3

Y1 - 2021/5/3

N2 - 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.

AB - 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.

U2 - 10.1039/D1OB00122A

DO - 10.1039/D1OB00122A

M3 - Article

JO - Organic & Biomolecular chemistry

JF - Organic & Biomolecular chemistry

SN - 1477-0520

ER -

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

Abstract

Access to Document

A National Network for Applications of High-Field NMR in the Life and Physical Sciences

Cite this

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