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Carbon Dioxide Hydration Activity of Carbonic Anhydrase: Paradoxical Consequences of the Unusually Rapid Catalysis

机译:碳酸酐酶的二氧化碳水化活性:异常迅速催化的矛盾后果

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摘要

The kinetic parameters for carbon dioxide hydration catalysis by carbonic anhydrase (EC 4.2.1.1) present an apparent paradox. The assumption of H2CO3 as the hydration product requires the rate of recombination of H2CO3 with enzyme to be faster than the diffusion limit. The alternative assumption of HCO3- as the product of hydration likewise requires active-site ionization rates to exceed the diffusion limit. We previously postulated the presence of special means for rapid active-site ionization. It is shown here that when proton transfer between enzyme and buffer species is taken into account, there is no need to invoke rates exceeding the diffusion limit. Bicarbonate ion thus appears as the most probable hydration product and dehydration substrate.
机译:碳酸酐酶催化的二氧化碳水合反应的动力学参数(EC 4.2.1.1)表现出明显的悖论。假设H2CO3是水合产物,则要求H2CO3与酶的复合速率快于扩散极限。作为水合产物的HCO3 -的替代假设同样要求活性位点电离速率超过扩散极限。我们之前曾假设存在用于快速活性部位电离的特殊方法。此处显示出,当考虑到酶和缓冲物质之间的质子转移时,不需要调用超过扩散极限的速率。因此,碳酸氢根离子似乎是最可能的水合产物和脱水底物。

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