Abstract
Thermolysin (E.C. 3.4.24.4) shows a remarkable increase in catalytic activity at elevated salt concentrations or hydrostatic pressures. Salt effected Kcat, only, whilst the effect of pressure was related to both Kcat, and Km. The turnover, derived from kcat/Km(V), of the hydrolysis of an N-acyldipeptide amide substrate was scarcely affected by addition of salt. These results were interpreted in terms of the stabilization of increased (or exposed) charges at the transition state of the reaction.
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