Problem 60
Draw Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. $$\begin{array}{ccc}{[\mathrm{S}]} & V, \text { No Inhibitor } & V, \text { Inhibitor Present } \\\\(\mathrm{mM}) & \left(\mathrm{mmol} \mathrm{min}^{-1}\right) & \left(\mathrm{mmol} \mathrm{min}^{-1}\right) \\\3.0 & 4.58 & 3.66 \\\5.0 & 6.40 & 5.12 \\\7.0 & 7.72 & 6.18 \\ 9.0 & 8.72 & 6.98 \\\11.0 & 9.50 & 7.60 \\\\\hline\end{array}$$ What are the \(K_{\mathrm{M}}\) and \(V_{\max }\) values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive?
Problem 65
Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by noncovalent interactions? Why?
Problem 66
Would you expect the structure of a noncompetitive inhibitor of a given enzyme to be similar to that of its substrate?