Akademik Veri Yönetim Sistemi
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.27, sa.1, ss.148-154, 2012 (SCI-Expanded)
Carbonic anhydrases (CA) catalyze activated ester hydrolysis in addition to the hydration of CO 2 to bicarbonate. They also show phosphatase activity with 4-nitrophenyl phosphate as substrate but not sulfatase with the corresponding sulfate. Here we prove that the enzyme is catalyzing the synthesis of cyclic diols from sulfate esters. 5-, 6- and 8-membered ring cyclic sulfates incorporating a neighboring secondary alcohol moiety were treated with CA II and yielded the corresponding cyclic diols. Inhibitory properties of obtained cyclic and original sulfate esters were then investigated on human carbonic anhydrase I (hCA I), hCA II, hCA IV and hCA VI (h = human isoform). K-I-s of these compounds ranged between 32.7-423 mu M against hCA I, 2.13-32.4 mu M against hCA II, 13.7-234 mu M against hCA IV and 76-278 mu M against CA VI, respectively. The sulfatase activity of CA with such esters is amazing considering the fact that 4-nitrophenyl-sulfate is not a substrate of these enzymes.