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

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Kose L. P., Gülçin İ., Yıldırım A., Atmaca U., Çelik M., Alwasel S. H., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.6, ss.1248-1253, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 6
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1120723
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1248-1253
  • Anahtar Kelimeler: Acetate, alcohol, carbonic anhydrase, enzyme inhibition, enzyme purification, hydroperoxide, TROUT ONCORHYNCHUS-MYKISS, ACETYLCHOLINE ESTERASE INHIBITORS, ERYTHROCYTE ISOZYMES I, BRASSICA-OLERACEA L., ANTIOXIDANT ACTIVITY, ISOFORMS I, BIOCHEMICAL-CHARACTERIZATION, SULFONAMIDE DERIVATIVES, LACTOPEROXIDASE ENZYME, PHENOLIC-COMPOUNDS
  • Atatürk Üniversitesi Adresli: Evet

Özet

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).