Simple methanesulfonates are hydrolyzed by the sulfatase carbonic anhydrase activity.

Elif Akin Kazancioğlu, Murat Güney, Murat Şentürk, Claudiu T Supuran

Department of Chemistry, Art and Science Faculty, Ağri Ibrahim Çeçen University, Ağri, Turkey.

Journal of enzyme inhibition and medicinal chemistry 2012 Dec

filter terms:

The possible sulfatase activity of several carbonic anhydrase (CA, EC 4.2.1.1) isoforms have been investigated with a series of synthesized methanesulfonate derivatives of phenols. Four α-CA isozymes, i.e. hCA I, hCA II, hCA IV and hCA VI (h = human isoform), were included in the study. We evidenced that the original sulfonate esters are being hydrolyzed effectively to the corresponding phenols which there after act as CA inhibitors. The K(I)-s of these compounds ranged from 10.24 to 4012 µM against hCA I, 0.10 to 35.42 µM against hCA II, 0.49 to 45.06 µM against hCA IV and 3.27 to 608 µM against CA VI, respectively. The relevant sulfatase activity of CA with these esters is amazing considering the fact that 4-nitrophenyl-sulfate, an activated ester, is not a substrate of these enzymes.

Citation

Elif Akin Kazancioğlu, Murat Güney, Murat Şentürk, Claudiu T Supuran. Simple methanesulfonates are hydrolyzed by the sulfatase carbonic anhydrase activity. Journal of enzyme inhibition and medicinal chemistry. 2012 Dec;27(6):880-5