Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/136015
Citations | ||
Scopus | Web of Science® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | Biosynthesis of uridine diphosphate N-Acetylglucosamine: An underexploited pathway in the search for novel antibiotics? |
Author: | Wyllie, J.A. McKay, M.V. Barrow, A.S. Soares da Costa, T.P. |
Citation: | IUBMB Life, 2022; 71(12):1232-1252 |
Publisher: | Wiley |
Issue Date: | 2022 |
ISSN: | 1521-6543 1521-6551 |
Statement of Responsibility: | Jessica A. Wyllie, Mirrin V. McKay, Andrew S. Barrow, Tatiana P. Soares da Costa |
Abstract: | Although the prevalence of antibiotic resistance is increasing at an alarmingrate, there are a dwindling number of effective antibiotics available. Thus, the development of novel antibacterial agents should be of utmost importance.Peptidoglycan biosynthesis has been and is still an attractive source for antibi-otic targets; however, there are several components that remain underex-ploited. In this review, we examine the enzymes involved in the biosynthesis of one such component, UDP-N-acetylglucosamine, an essential building block and precursor of bacterial peptidoglycan. Furthermore, given the presence of a similar biosynthesis pathway in eukaryotes, we discuss the current knowledge on the differences and similarities between the bacterial and eukaryoticenzymes. Finally, this review also summarises the recent advances made in the development of inhibitors targeting the bacterial enzymes. |
Keywords: | antibiotic resistance; bifunctional GlmU; glucosamine-6-phosphate synthase; peptidoglycan biosynthesis; phosphoglucosamine mutase; UDP-N-acetylglucosamine biosynthesis |
Description: | Published December 2022 |
Rights: | © 2022 The Authors.IUBMB Life published by Wiley Periodicals LLC on behalf of International Union of Biochemistry and Molecular Biology.This is an open access article under the terms of theCreative Commons Attribution-NonCommercialLicense, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
DOI: | 10.1002/iub.2664 |
Grant ID: | http://purl.org/au-research/grants/arc/DP220101901 http://purl.org/au-research/grants/arc/DE19100806 |
Published version: | http://dx.doi.org/10.1002/iub.2664 |
Appears in Collections: | Molecular and Biomedical Science publications |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
hdl_136015.pdf | Published version | 10.25 MB | Adobe PDF | View/Open |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.