Drug-biomolecule interactions: topographical study of active site of erythrocyte carbonic anhydrase using spin-labeled sulfanilamide drugs.
The topography of the active sites of human erythrocyte carbonic anhydrases B and C and bovine erythrocyte carbonic anhydrase B was studied using a series of spin-labeled sulfanilamide analogs. Results show that the active site of human carbonic anhydrase C is a narrow cleft approximately 14 A in depth. This observation is in good agreement with previously published X-ray diffraction data. While the active sites of human carbonic anhydrase B and bovine carbonic anhydrase B have the same general shape as the active site of human carbonic anhydrase C, they are slightly deeper.
D001593:Benzyl Compounds; D001665:Binding Sites / Q000187:drug effects; D002256:Carbonic Anhydrases / Q000097:blood*; D004912:Erythrocytes / Q000201:enzymology*; D005609:Free Radicals; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009589:Nitrogen Oxides; D011487:Protein Conformation; D011759:Pyrrolidines; D013113:Spin Labels; D013424:Sulfanilamides / Q000097:blood*; D013438:Sulfhydryl Compounds
D001593:Benzyl Compounds; D005609:Free Radicals; D009589:Nitrogen Oxides; D011759:Pyrrolidines; D013113:Spin Labels; D013424:Sulfanilamides; D013438:Sulfhydryl Compounds; D002256:Carbonic Anhydrases