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The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives
Carbonic anhydrase is a ubiquitous metalloenzyme, which catalyzes the reversible hydration of CO(2) to HCO(3)(−) and H(+). Metals play a key role in the bioactivity of this metalloenzyme, although their relationships with CA have not been completely clarified to date. The aim of this review is to ex...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730368/ https://www.ncbi.nlm.nih.gov/pubmed/26797606 http://dx.doi.org/10.3390/ijms17010127 |
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author | Lionetto, Maria Giulia Caricato, Roberto Giordano, Maria Elena Schettino, Trifone |
author_facet | Lionetto, Maria Giulia Caricato, Roberto Giordano, Maria Elena Schettino, Trifone |
author_sort | Lionetto, Maria Giulia |
collection | PubMed |
description | Carbonic anhydrase is a ubiquitous metalloenzyme, which catalyzes the reversible hydration of CO(2) to HCO(3)(−) and H(+). Metals play a key role in the bioactivity of this metalloenzyme, although their relationships with CA have not been completely clarified to date. The aim of this review is to explore the complexity and multi-aspect nature of these relationships, since metals can be cofactors of CA, but also inhibitors of CA activity and modulators of CA expression. Moreover, this work analyzes new insights and perspectives that allow translating new advances in basic science on the interaction between CA and metals to applications in several fields of research, ranging from biotechnology to environmental sciences. |
format | Online Article Text |
id | pubmed-4730368 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-47303682016-02-11 The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives Lionetto, Maria Giulia Caricato, Roberto Giordano, Maria Elena Schettino, Trifone Int J Mol Sci Review Carbonic anhydrase is a ubiquitous metalloenzyme, which catalyzes the reversible hydration of CO(2) to HCO(3)(−) and H(+). Metals play a key role in the bioactivity of this metalloenzyme, although their relationships with CA have not been completely clarified to date. The aim of this review is to explore the complexity and multi-aspect nature of these relationships, since metals can be cofactors of CA, but also inhibitors of CA activity and modulators of CA expression. Moreover, this work analyzes new insights and perspectives that allow translating new advances in basic science on the interaction between CA and metals to applications in several fields of research, ranging from biotechnology to environmental sciences. MDPI 2016-01-19 /pmc/articles/PMC4730368/ /pubmed/26797606 http://dx.doi.org/10.3390/ijms17010127 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Lionetto, Maria Giulia Caricato, Roberto Giordano, Maria Elena Schettino, Trifone The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title | The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title_full | The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title_fullStr | The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title_full_unstemmed | The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title_short | The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives |
title_sort | complex relationship between metals and carbonic anhydrase: new insights and perspectives |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730368/ https://www.ncbi.nlm.nih.gov/pubmed/26797606 http://dx.doi.org/10.3390/ijms17010127 |
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