The human carbonic anhydrase isoenzymes I and II inhibitory effects of some hydroperoxides, alcohols, and acetates. (1st November 2016)

• Record Type: Journal Article
• Authors: Kose, Leyla Polat; Gulcin, İlhami; Yıldırım, Alper; Atmaca, Ufuk; Çelik, Murat; Alwasel, Saleh H.; Supuran, Claudiu T.
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 31:Number 6(2016:Dec.)
• Page Start: 1248
• Page End: 1253
• Publication Date: 2016-11-01
• Subjects: Acetate -- alcohol -- carbonic anhydrase -- enzyme inhibition -- enzyme purification -- hydroperoxide; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.3109/14756366.2015.1120723
• Languages: English
• ISSNs: 1475-6366

Abstract

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 ( Ki s in the range of 24.93–97.99 nM) and hCA II inhibitors ( Ki s 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).