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Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii
Burkholderia territorii, a Gram-negative bacterium, encodes for the ι-class carbonic anhydrase (CA, EC 4.2.1.1) BteCAι, which was recently characterised. It acts as a good catalyst for the hydration of CO(2) to bicarbonate and protons, with a k(cat) value of 3.0 × 10(5) s(−1) and k(cat)/K(M) value o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Taylor & Francis
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7782983/ https://www.ncbi.nlm.nih.gov/pubmed/33390061 http://dx.doi.org/10.1080/14756366.2020.1867122 |
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author | Petreni, Andrea De Luca, Viviana Scaloni, Andrea Nocentini, Alessio Capasso, Clemente Supuran, Claudiu T. |
author_facet | Petreni, Andrea De Luca, Viviana Scaloni, Andrea Nocentini, Alessio Capasso, Clemente Supuran, Claudiu T. |
author_sort | Petreni, Andrea |
collection | PubMed |
description | Burkholderia territorii, a Gram-negative bacterium, encodes for the ι-class carbonic anhydrase (CA, EC 4.2.1.1) BteCAι, which was recently characterised. It acts as a good catalyst for the hydration of CO(2) to bicarbonate and protons, with a k(cat) value of 3.0 × 10(5) s(−1) and k(cat)/K(M) value of 3.9 × 10(7) M(−1) s(−1). No inhibition data on this new class of enzymes are available to date. We report here an anion and small molecules inhibition study of BteCAι, which we prove to be a zinc(II)- and not manganese(II)-containing enzyme, as reported for diatom ι-CAs. The best inhibitors were sulphamic acid, stannate, phenylarsonic acid, phenylboronic acid and sulfamide (K(I) values of 6.2–94 µM), whereas diethyldithiocarbamate, tellurate, selenate, bicarbonate and cyanate were submillimolar inhibitors (K(I) values of 0.71–0.94 mM). The halides (except iodide), thiocyanate, nitrite, nitrate, carbonate, bisulphite, sulphate, hydrogensulfide, peroxydisulfate, selenocyanate, fluorosulfonate and trithiocarbonate showed K(I) values in the range of 3.1–9.3 mM. |
format | Online Article Text |
id | pubmed-7782983 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-77829832021-01-14 Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii Petreni, Andrea De Luca, Viviana Scaloni, Andrea Nocentini, Alessio Capasso, Clemente Supuran, Claudiu T. J Enzyme Inhib Med Chem Research Paper Burkholderia territorii, a Gram-negative bacterium, encodes for the ι-class carbonic anhydrase (CA, EC 4.2.1.1) BteCAι, which was recently characterised. It acts as a good catalyst for the hydration of CO(2) to bicarbonate and protons, with a k(cat) value of 3.0 × 10(5) s(−1) and k(cat)/K(M) value of 3.9 × 10(7) M(−1) s(−1). No inhibition data on this new class of enzymes are available to date. We report here an anion and small molecules inhibition study of BteCAι, which we prove to be a zinc(II)- and not manganese(II)-containing enzyme, as reported for diatom ι-CAs. The best inhibitors were sulphamic acid, stannate, phenylarsonic acid, phenylboronic acid and sulfamide (K(I) values of 6.2–94 µM), whereas diethyldithiocarbamate, tellurate, selenate, bicarbonate and cyanate were submillimolar inhibitors (K(I) values of 0.71–0.94 mM). The halides (except iodide), thiocyanate, nitrite, nitrate, carbonate, bisulphite, sulphate, hydrogensulfide, peroxydisulfate, selenocyanate, fluorosulfonate and trithiocarbonate showed K(I) values in the range of 3.1–9.3 mM. Taylor & Francis 2021-01-04 /pmc/articles/PMC7782983/ /pubmed/33390061 http://dx.doi.org/10.1080/14756366.2020.1867122 Text en © 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://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/ (https://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 Petreni, Andrea De Luca, Viviana Scaloni, Andrea Nocentini, Alessio Capasso, Clemente Supuran, Claudiu T. Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title | Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title_full | Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title_fullStr | Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title_full_unstemmed | Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title_short | Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii |
title_sort | anion inhibition studies of the zn(ii)-bound ι-carbonic anhydrase from the gram-negative bacterium burkholderia territorii |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7782983/ https://www.ncbi.nlm.nih.gov/pubmed/33390061 http://dx.doi.org/10.1080/14756366.2020.1867122 |
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