Question 4 In this problem three different types of reaction inhibition are explored: (a) In competitive inhibition, an inhibitor adsorbs on the same type of site as the substrate. The resulting inhibitor-enzyme complex is inactive. Show that the rate law for competitive inhibition E+SE E-S E+17 PEI E-S is the rate law is (b) In uncompetitive inhibition the inhibitor attaches itself to enzyme-substrate complex, rendering it inactive. Show that for uncompetitive inhibition, E + S E-S I + E.S IES E-S > P+E VIS max S+K(1+I/K) the rate law is E + P (c) In noncompetitive inhibition, the inhibitor adsorbs itself to a different type of site than the substrate to render the enzyme-substrate complex inactive. Assuming that all concentrations of a species can be expressed by their equilibrium concentrations, show that for noncompetitive inhibition IE E +I Vmax S Km+S(1+I/K) ES P+E IES Vmax S (S+ KM)(1+I/K) (d) Sketch three different inhibitions on a Lineweaver-Burk plot.