STUDIES ON THE ENZYME KINETICS OF THE CAVITY-ACTIVE SITE
摘要
The results of X-ray diffraction analysis have shown that, in the great majority of cases, the enzymatic active site is situated in a concave region, the molecular crevice. For such enzymatic reaction systems the reaction can take place only when the substrate molecules come into the cavity. The present investigation was initiated in an attempt to study the kinetic process of catalysis in a cavity. The results obtained by applying equations derived in this paper indicate that the active site being situated in a cavity does not generally bring about appreciable reduction in the reaction rates of bimolecular steps between enzyme and substrate. This not only resolves the paradox encountered in investigations into the reaction mechanism for carbonic anhydrase, but also furnishes an example of dialectical unity between molecular structure and function.