Abstract
A scheme, previously proposed for the catalytic mechanism of carbonic anhydrase, has been tested by computer simulations of steady-state kinetic patterns. The scheme contains two ionizing active-site groups. One of them is involved in the interconversion between CO 2 and HCO 3 − The other group is involved in the transfer of H + between the active site and the reaction medium. In human carbonic anhydrase II (or C) an intramolecular H + transfer between the groups limits the rate of turnover. The computer-generated patterns of pH dependence, dependence on buffer concentration, inhibition by anions and by phenol are in accordance with experimental results. Deviations from Michaelis-Menten kinetics observed in the hydration of CO 2 catalyzed by human carbonic anhydrase I (or B) under certain conditions are also mimicked by computer simulations. It is concluded that the proposed scheme is a satisfactory model for the catalytic mechanisms of the human isoenzymes I and II.
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