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• W2144256341 abstract "Enzyme inhibition assays often require deviations from physiological conditions. For carbonic anhydrases, procedures involving native CO 2 and non‐native substrates have been used. We compared a native and a non‐native substrate in the context of inhibition of human carbonic anhydrases I and II by examining various sulfamate and sulfamide compounds in two kinetic assays: hydration of CO 2 and hydrolysis of 4‐nitrophenylacetate. For carbonic anhydrase II, the two assays consistently generated similar K i values, with the relative difference between the assays never exceeding 2.5‐fold. However, for carbonic anhydrase I there was more variability between the two assays, with K i values for three compounds differing by more than 2.5‐fold, up to eightfold. In the CO 2 hydration assay, some sulfamates and sulfamides exhibited mixed kinetics or partial inhibition. Our results indicate that K i or K d values from carbonic anhydrase assays involving non‐native substrates should be confirmed by assays that use CO 2 (or HCO ), to establish pharmacological relevance. From structure–activity comparisons, the sulfamate is more effective than the sulfamide in inhibiting carbonic anhydrase I and II, but the sulfamate does not confer selectivity. In contrast, the sulfonamide confers selectivity for carbonic anhydrase I (10‐ to 30‐fold). Selectivity for carbonic anhydrase II occurred with the substituted fructose moiety, especially the d ‐enantiomer (>100‐fold)." @default.
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• W2144256341 date "2006-08-01" @default.
• W2144256341 modified "2023-10-16" @default.
• W2144256341 title "Examination of Two Independent Kinetic Assays for Determining the Inhibition of Carbonic Anhydrases I and II: Structure?Activity Comparison of Sulfamates and Sulfamides" @default.
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• W2144256341 doi "https://doi.org/10.1111/j.1747-0285.2006.00423.x" @default.
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