The human carbonic anhydrase isoenzymes I and II inhibitory effects of some hydroperoxides, alcohols, and acetates

  • J Enzyme Inhib Med Chem. 2016 Dec;31(6):1248-53. doi: 10.3109/14756366.2015.1120723.
Leyla Polat Kose  1 ,  İlhami Gulcin  1  2 ,  Alper Yıldırım  1 ,  Ufuk Atmaca  1 ,  Murat Çelik  1 ,  Saleh H Alwasel  2 ,  Claudiu T Supuran  3  4
Affiliations
  • 1. a Department of Chemistry, Faculty of Sciences , Atatürk University , Erzurum , Turkey .
  • 2. b Department of Zoology , College of Science, King Saud University , Saudi Arabia .
  • 3. c Dipartimento Di Chimica Ugo Schiff , Università Degli Studi Di Firenze , Firenze , Italy , and.
  • 4. d Neurofarba Department , Section of Pharmaceutical and Nutriceutical Sciences, Università Degli Studi Di Firenze , Florence , Italy.
PMID: 26677909 DOI: 10.3109/14756366.2015.1120723
Abstract

The carbonic anhydrases (CAs, EC 4.2.1.1) represent a superfamily of widespread Enzymes, which catalyze a crucial biochemical reaction, the reversible hydration of carbon dioxide to bicarbonate and protons. Human CA isoenzymes I and II (hCA I and hCA II) are ubiquitous cytosolic isoforms. In this study, a series of hydroperoxides, alcohols, and acetates were tested for the inhibition of the cytosolic hCA I and II isoenzymes. These compounds inhibited both hCA isozymes in the low nanomolar ranges. These compounds were good hCA I inhibitors (Kis in the range of 24.93-97.99 nM) and hCA II inhibitors (Kis in the range of 26.04-68.56 nM) compared to acetazolamide as CA Inhibitor (Ki: 34.50 nM for hCA I and Ki: 28.93 nM for hCA II).

Keywords
Acetate; alcohol; carbonic anhydrase; enzyme inhibition; enzyme purification; hydroperoxide.