The human carbonic anhydrase isoenzymes I and II inhibitory effects of some hydroperoxides, alcohols, and acetates
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.6, ss.1248-1253, 2016 (SCI-Expanded, Scopus)
- 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
- Açık Arşiv Koleksiyonu: AVESİS Açık Erişim Koleksiyonu
- 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).