Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES complex also undergoes suicidal inactivation that would result in the loss of the total enzyme activity. In addition, after the binding of S to E there exposes another binding site in E for uncompetitive inhibitor I. The ESI complex does not have the capacity to form product and would not undergo inactivation. The equilibriums, reactions and the kinetic parameters involved can be represented as follows: Ks KI E + S ←→ ES + I ←→ ESI ki E-S(inactive) a. Derive the integrated rate equation for the loss of enzyme activity In Eo [Eapp xt, where kapp is a function of ki, [S], [I, Ks and Ki b. Assume [S] Ks,plot In enzyme activity vs time at increasing [I] Enzyme E bind to substrate S to form ES complex leading to product formation. However, the ES complex also undergoes suicidal inactivation that would result in the loss of the total enzyme activity. In addition, after the binding of S to E there exposes another binding site in E for uncompetitive inhibitor I. The ESI complex does not have the capacity to form product and would not undergo inactivation. The equilibriums, reactions and the kinetic parameters involved can be represented as follows: Ks KI E + S ←→ ES + I ←→ ESI ki E-S(inactive) a. Derive the integrated rate equation for the loss of enzyme activity In Eo [Eapp xt, where kapp is a function of ki, [S], [I, Ks and Ki b. Assume [S] Ks,plot In enzyme activity vs time at increasing [I]