Question

b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing for the active site.

Answer 1

solution

Que c) Vmax of enzyme is not changed it will remain same in compititive inhibition as like without inhibitor.because when compitive inhibitor binds to enzymes active site it compets with substrate so as concentration kept high of inhibitor at all time.hence enzyme get saturated completely.if concentration of inhinitor drop downs that time rate of velosity of reaction increases.

Que d) Vmax/2 will not affected but substrate concentration require to achieve Vmax/2 is get changed. Becuase according to graph shown as Vmax is not changing hence Vmax/2 will also not changing.

que e)the km is affected that is km value wil increases in compititve inhibition. Km is substrate concentration required to attain Vmax/2 (half maximum velosity). So if km is increased so it enzyme required more substrate concentration because at  high km value affinity of substrate to enzyme decreases while at low km value affinity of substrate to enzyme will increases.

as inhibitor comptes for active site substrate affinity will decreases towards enzyme so km will increases.