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Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei

The β-class carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic bacterium Burkholderia pseudomallei, BpsCAβ, that is responsible for the tropical disease melioidosis was investigated for its activation with natural and non-natural amino acids and amines. Previously, the γ-CA from this bacterium...

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Autores principales: Vullo, Daniela, Del Prete, Sonia, Osman, Sameh M., Alasmary, Fatmah A. S., AlOthman, Zeid, Donald, William A., Capasso, Clemente, Supuran, Claudiu T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6009869/
https://www.ncbi.nlm.nih.gov/pubmed/29098887
http://dx.doi.org/10.1080/14756366.2017.1387544
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author Vullo, Daniela
Del Prete, Sonia
Osman, Sameh M.
Alasmary, Fatmah A. S.
AlOthman, Zeid
Donald, William A.
Capasso, Clemente
Supuran, Claudiu T.
author_facet Vullo, Daniela
Del Prete, Sonia
Osman, Sameh M.
Alasmary, Fatmah A. S.
AlOthman, Zeid
Donald, William A.
Capasso, Clemente
Supuran, Claudiu T.
author_sort Vullo, Daniela
collection PubMed
description The β-class carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic bacterium Burkholderia pseudomallei, BpsCAβ, that is responsible for the tropical disease melioidosis was investigated for its activation with natural and non-natural amino acids and amines. Previously, the γ-CA from this bacterium has been investigated with the same library of 19 amines/amino acids, which show very potent activating effects on both enzymes. The most effective BpsCAβ activators were L- and D-DOPA, L- and D-Trp, L-Tyr, 4-amino-L-Phe, histamine, dopamine, serotonin, 2-pyridyl-methylamine, 1-(2-aminoethyl)-piperazine and L-adrenaline with K(A)s of 0.9–27 nM. Less effective activators were D-His, L- and D-Phe, D-Tyr, 2-(2-aminoethyl)pyridine and 4-(2-aminoethyl)-morpholine with K(A)s of 73 nM–3.42 µM. The activation of CAs from bacteria, such as BpsCAγ/β, has not been considered previously for possible biomedical applications. It would be of interest to perform studies in which bacteria are cultivated in the presence of CA activators, which may contribute to understanding processes connected with the virulence and colonization of the host by pathogenic bacteria.
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spelling pubmed-60098692018-07-11 Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei Vullo, Daniela Del Prete, Sonia Osman, Sameh M. Alasmary, Fatmah A. S. AlOthman, Zeid Donald, William A. Capasso, Clemente Supuran, Claudiu T. J Enzyme Inhib Med Chem Research Paper The β-class carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic bacterium Burkholderia pseudomallei, BpsCAβ, that is responsible for the tropical disease melioidosis was investigated for its activation with natural and non-natural amino acids and amines. Previously, the γ-CA from this bacterium has been investigated with the same library of 19 amines/amino acids, which show very potent activating effects on both enzymes. The most effective BpsCAβ activators were L- and D-DOPA, L- and D-Trp, L-Tyr, 4-amino-L-Phe, histamine, dopamine, serotonin, 2-pyridyl-methylamine, 1-(2-aminoethyl)-piperazine and L-adrenaline with K(A)s of 0.9–27 nM. Less effective activators were D-His, L- and D-Phe, D-Tyr, 2-(2-aminoethyl)pyridine and 4-(2-aminoethyl)-morpholine with K(A)s of 73 nM–3.42 µM. The activation of CAs from bacteria, such as BpsCAγ/β, has not been considered previously for possible biomedical applications. It would be of interest to perform studies in which bacteria are cultivated in the presence of CA activators, which may contribute to understanding processes connected with the virulence and colonization of the host by pathogenic bacteria. Taylor & Francis 2017-11-03 /pmc/articles/PMC6009869/ /pubmed/29098887 http://dx.doi.org/10.1080/14756366.2017.1387544 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 Research Paper
Vullo, Daniela
Del Prete, Sonia
Osman, Sameh M.
Alasmary, Fatmah A. S.
AlOthman, Zeid
Donald, William A.
Capasso, Clemente
Supuran, Claudiu T.
Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title_full Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title_fullStr Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title_full_unstemmed Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title_short Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei
title_sort comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium burkholderia pseudomallei
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6009869/
https://www.ncbi.nlm.nih.gov/pubmed/29098887
http://dx.doi.org/10.1080/14756366.2017.1387544
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