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Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes
Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO(2)) and water (H(2)O) into a proton (H(+)) and bicarbonate (HCO(3)(–)) ion. On the other hand, capsaicin is the main component in hot chili peppers and is u...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270996/ https://www.ncbi.nlm.nih.gov/pubmed/25014536 http://dx.doi.org/10.3390/molecules190710103 |
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author | Arabaci, Betul Gulcin, Ilhami Alwasel, Saleh |
author_facet | Arabaci, Betul Gulcin, Ilhami Alwasel, Saleh |
author_sort | Arabaci, Betul |
collection | PubMed |
description | Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO(2)) and water (H(2)O) into a proton (H(+)) and bicarbonate (HCO(3)(–)) ion. On the other hand, capsaicin is the main component in hot chili peppers and is used extensively used in spices, food additives and drugs; it is responsible for their spicy flavor and pungent taste. There are sixteen known CA isoforms in humans. Human CA isoenzymes I, and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of capsaicin against the slow cytosolic isoform hCA I, and the ubiquitous and dominant rapid cytosolic isozymes hCA II were studied. Both CA isozymes were inhibited by capsaicin in the micromolar range. This naturally bioactive compound has a Ki of 696.15 µM against hCA I, and of 208.37 µM against hCA II. |
format | Online Article Text |
id | pubmed-6270996 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62709962018-12-21 Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes Arabaci, Betul Gulcin, Ilhami Alwasel, Saleh Molecules Article Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO(2)) and water (H(2)O) into a proton (H(+)) and bicarbonate (HCO(3)(–)) ion. On the other hand, capsaicin is the main component in hot chili peppers and is used extensively used in spices, food additives and drugs; it is responsible for their spicy flavor and pungent taste. There are sixteen known CA isoforms in humans. Human CA isoenzymes I, and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. In this study, the inhibition properties of capsaicin against the slow cytosolic isoform hCA I, and the ubiquitous and dominant rapid cytosolic isozymes hCA II were studied. Both CA isozymes were inhibited by capsaicin in the micromolar range. This naturally bioactive compound has a Ki of 696.15 µM against hCA I, and of 208.37 µM against hCA II. MDPI 2014-07-10 /pmc/articles/PMC6270996/ /pubmed/25014536 http://dx.doi.org/10.3390/molecules190710103 Text en © 2014 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Arabaci, Betul Gulcin, Ilhami Alwasel, Saleh Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title | Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title_full | Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title_fullStr | Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title_full_unstemmed | Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title_short | Capsaicin: A Potent Inhibitor of Carbonic Anhydrase Isoenzymes |
title_sort | capsaicin: a potent inhibitor of carbonic anhydrase isoenzymes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270996/ https://www.ncbi.nlm.nih.gov/pubmed/25014536 http://dx.doi.org/10.3390/molecules190710103 |
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