capsaicin: a potent inhibitor of carbonic anhydrase isoenzymes

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ID: 210755
2014
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Abstract
Carbonic anhydrase (CA, EC 4.2.1.1) is a zinc containing metalloenzyme that catalyzes the rapid and reversible conversion of carbon dioxide (CO2) and water (H2O) into a proton (H+) and bicarbonate (HCO3–) 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.
Reference Key
arabaci2014moleculescapsaicin: Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Betul Arabaci;Ilhami Gulcin;Saleh Alwasel
Journal Journal of ethnopharmacology
Year 2014
DOI
10.3390/molecules190710103
URL
http://www.mdpi.com/1420-3049/19/7/10103
Keywords
enzyme inhibition carbonic anhydrase capsaicin enzyme purification

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