. Biophysical science. Biophysics. 322 Enzyme Kinetics of Hydrolytic Reactions /I7 : 3 complex E-S. The complex E-S was assumed to be in quasi-equilibrium with E and S, but also to break down to form the products. The reaction then would follow the scheme e-p xk p E + S^±E-S E-S + H20 -^ E + Products where the letters above the reactants will be used to denote concen- trations, thereby avoiding need for the square brackets. Note that e is. Figure 3. The rate at which a substrate S is hydrolyzed as a function of substrate concentra- tion. Curves are plotted for three concentrations of the enzym

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. Biophysical science. Biophysics. 322 Enzyme Kinetics of Hydrolytic Reactions /I7 : 3 complex E-S. The complex E-S was assumed to be in quasi-equilibrium with E and S, but also to break down to form the products. The reaction then would follow the scheme e-p xk p E + S^±E-S E-S + H20 -^ E + Products where the letters above the reactants will be used to denote concen- trations, thereby avoiding need for the square brackets. Note that e is. Figure 3. The rate at which a substrate S is hydrolyzed as a function of substrate concentra- tion. Curves are plotted for three concentrations of the enzyme E. Note that all three curves reach half maximum velocity at [S] = Km- </[S] dt. Please note that these images are extracted from scanned page images that may have been digitally enhanced for readability - coloration and appearance of these illustrations may not perfectly resemble the original Ackerman, Eugene, 1920-. Englewood Cliffs, N. J. , Prentice-Hall

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