The effects of some bromophenols on human carbonic anhydrase isoenzymes

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1), which are involved in a variety of physiological and pathological processes, are ubiquitous metalloenzymes mainly catalyzing the reversible hydration of carbon dioxide (CO₂) to bicarbonate () and proton (H⁺). In this study, a dozen of bromophenol derivatives (1–12) were evaluated as metalloenzyme CA (EC 4.2.1.1) inhibitors against the human carbonic anhydrase isoenzymes I and II (hCA I and II). Cytosolic hCA I and II isoenzymes were effectively inhibited by bromophenol derivatives (1–12) with K_is in the low nanomolar range of 1.85 ± 0.58 to 5.04 ± 1.46 nM against hCA I and in the range of 2.01 ± 0.52 to 2.94 ± 1.31 nM against hCA II, respectively.

• Bromophenols
• carbonic anhydrase
• enzyme inhibition
• enzyme purification
• isoenzymes

Acknowledgement

I.G. and S.H.A. would like to extend their sincere appreciation to the Research Chairs Program at King Saud University for funding this research.

Declaration of interest

The authors report there is no conflict of interests.