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- W2087864300 abstract "We studied anionic inhibition of the reaction CO2 + OH−⇄ HCO3− catalyzed by human red cell carbonic anhydrase B (I) and C (II), using iodide and cyanate. In the forward reaction with respect to CO2 as the substrate, inhibition was mixed but favoring noncompetitive; the back reaction, with HCO3− as the substrate, yielded strict competitive kinetics. Mean inhibition constants, KI, in the pH range 7.2–7.5 are: iodide, 0.5 mm for enzyme B and 16 mm for C; cyanate, 0.8 μm for B and 20 μm for C. When OH− was considered as the substrate for the forward reaction, cyanate and chloride behaved as competitive inhibitors. The true inhibition constant (KI0) for cyanate (calculated for infinitely low OH−) is 0.4 μm for enzyme B and 4 μm for C. Apart from the difference in anion affinity and some 10-fold higher activity of C > B, the isozymes showed similar patterns of inhibition. Data agree with generally proposed mechanisms describing the active site as ZnH2O with pKa of about 7." @default.
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- W2087864300 title "The nature of anion inhibition of human red cell carbonic anhydrases" @default.
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- W2087864300 doi "https://doi.org/10.1016/0003-9861(79)90302-3" @default.
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