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Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?

Carbonic anhydrases have started to emerge as new potential antibacterial targets for several pathogens. Two β-carbonic anhydrases, denominated bsCA I and bsCA II, have been isolated and characterized from the bacterial pathogen Brucella suis, the causative agent of brucellosis or Malta fever. These...

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Autores principales: Köhler, Stephan, Ouahrani-Bettache, Safia, Winum, Jean-Yves
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6009918/
https://www.ncbi.nlm.nih.gov/pubmed/28274160
http://dx.doi.org/10.1080/14756366.2017.1295451
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author Köhler, Stephan
Ouahrani-Bettache, Safia
Winum, Jean-Yves
author_facet Köhler, Stephan
Ouahrani-Bettache, Safia
Winum, Jean-Yves
author_sort Köhler, Stephan
collection PubMed
description Carbonic anhydrases have started to emerge as new potential antibacterial targets for several pathogens. Two β-carbonic anhydrases, denominated bsCA I and bsCA II, have been isolated and characterized from the bacterial pathogen Brucella suis, the causative agent of brucellosis or Malta fever. These enzymes have been investigated in detail and a wide range of classical aromatic and heteroaromatic sulfonamides as well as carbohydrate-based compounds have been found to inhibit selectively and efficiently Brucella suis carbonic anhydrases. Inhibition of these metalloenzymes constitutes a novel approach for the potential development of new anti-Brucella agents. This review aims at discussing the recent literature on this topic.
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spelling pubmed-60099182018-07-11 Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics? Köhler, Stephan Ouahrani-Bettache, Safia Winum, Jean-Yves J Enzyme Inhib Med Chem Review Article Carbonic anhydrases have started to emerge as new potential antibacterial targets for several pathogens. Two β-carbonic anhydrases, denominated bsCA I and bsCA II, have been isolated and characterized from the bacterial pathogen Brucella suis, the causative agent of brucellosis or Malta fever. These enzymes have been investigated in detail and a wide range of classical aromatic and heteroaromatic sulfonamides as well as carbohydrate-based compounds have been found to inhibit selectively and efficiently Brucella suis carbonic anhydrases. Inhibition of these metalloenzymes constitutes a novel approach for the potential development of new anti-Brucella agents. This review aims at discussing the recent literature on this topic. Taylor & Francis 2017-03-08 /pmc/articles/PMC6009918/ /pubmed/28274160 http://dx.doi.org/10.1080/14756366.2017.1295451 Text en © 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Köhler, Stephan
Ouahrani-Bettache, Safia
Winum, Jean-Yves
Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title_full Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title_fullStr Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title_full_unstemmed Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title_short Brucella suis carbonic anhydrases and their inhibitors: Towards alternative antibiotics?
title_sort brucella suis carbonic anhydrases and their inhibitors: towards alternative antibiotics?
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6009918/
https://www.ncbi.nlm.nih.gov/pubmed/28274160
http://dx.doi.org/10.1080/14756366.2017.1295451
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