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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doaj-8351873acd704de288c5a7474d7f96742020-11-25T01:52:52ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742018-01-01331253010.1080/14756366.2017.13875441387544Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomalleiDaniela Vullo0Sonia Del Prete1Sameh M. Osman2Fatmah A. S. Alasmary3Zeid AlOthman4William A. Donald5Clemente Capasso6Claudiu T. Supuran7Università degliStudi di FirenzeIstituto di Bioscienze e BiorisorseCollege of Science, King Saud UniversityCollege of Science, King Saud UniversityCollege of Science, King Saud UniversityUniversity of New South WalesIstituto di Bioscienze e BiorisorseUniversità degli Studi di FirenzeThe 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 KAs 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 KAs 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.http://dx.doi.org/10.1080/14756366.2017.1387544Carbonic anhydrasemetalloenzymespathogensactivatorsBurkholderia pseudomallei |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Daniela Vullo Sonia Del Prete Sameh M. Osman Fatmah A. S. Alasmary Zeid AlOthman William A. Donald Clemente Capasso Claudiu T. Supuran |
spellingShingle |
Daniela Vullo Sonia Del Prete Sameh M. Osman Fatmah A. S. Alasmary Zeid AlOthman William A. Donald Clemente Capasso Claudiu T. Supuran Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei Journal of Enzyme Inhibition and Medicinal Chemistry Carbonic anhydrase metalloenzymes pathogens activators Burkholderia pseudomallei |
author_facet |
Daniela Vullo Sonia Del Prete Sameh M. Osman Fatmah A. S. Alasmary Zeid AlOthman William A. Donald Clemente Capasso Claudiu T. Supuran |
author_sort |
Daniela Vullo |
title |
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_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_sort |
comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium burkholderia pseudomallei |
publisher |
Taylor & Francis Group |
series |
Journal of Enzyme Inhibition and Medicinal Chemistry |
issn |
1475-6366 1475-6374 |
publishDate |
2018-01-01 |
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 KAs 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 KAs 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. |
topic |
Carbonic anhydrase metalloenzymes pathogens activators Burkholderia pseudomallei |
url |
http://dx.doi.org/10.1080/14756366.2017.1387544 |
work_keys_str_mv |
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