Question

The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation.

b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km.

c). Please draw a plot of V0 versus V0/[S] in the presence and in the absence of a competitive inhibitor.

Answer 1

The Y axis intercept is the Vm and slope is negative Km.

c.

Given below is the Eadie-Hofstee plot for an enzyme kinetics in the presence and absence of a competitive inhibitor

As can be seen from the graph, the Vm value remained unchanged in the presence of competitive inhibitor, but the Km value is altered.