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 (K(i)s in the range of 24.93-97.99 nM) and hCA II inhibitors (K(i)s in the range of 26.04-68.56 nM) compared to acetazolamide as CA inhibitor (K-i: 34.50nM for hCA I and K-i: 28.93nM for hCA II).