Docking substrates to metalloenzymes

Carbonic Anhydrase (CA) is a metalloenzyme that reversibly catalyzes the in terconversion between carbon dioxide and bicarbonate anion. A class of sulf a drugs, sulfonamides, are known to inhibit CA. One approach to identifying important binding and specificity interactions between sulfonamides and CA is to analyze the results from docking studies. Previous docking studies h ave mainly focused on the encounters of substrates with non-metalloenzymes. Here we report the application of MOE-Dock to the CA II - sulfonamide syst em. After developing a standard docking protocol for the CA II - sulfonamid e system we then used the protocol to determine other CA II - sulfonamide c omplexes.