Final answer:
option a,In a plot of 1/V against 1/[S] for an enzyme-catalyzed reaction, the Lineweaver-Burk plot is obtained, which gives the values of 1/Vmax and 1/Km, providing insights into the enzyme's efficiency and substrate affinity.
Step-by-step explanation:
When plotting the inverse of the initial velocities (1/V) against the inverse of the corresponding substrate concentrations (1/[S]) in an enzyme-catalyzed reaction, you obtain a Lineweaver-Burk plot. This type of plot allows for the determination of two key kinetic parameters: Vmax and Km (Michaelis constant). The intercepts of the plot give the values of 1/Vmax and 1/Km, providing valuable information about the enzyme's efficiency and the affinity for its substrate. The Vmax indicates the maximum rate the enzyme can achieve when saturated with substrate, whereas Km reflects the substrate concentration at which the reaction rate is half of the Vmax. This plot is particularly useful for characterizing enzymes and understanding how they facilitate reactions.
This can be explained by using the Michaelis-Menten kinetics equation, which states that the initial velocity (V) of an enzyme-catalyzed reaction is proportional to the substrate concentration ([S]) divided by the sum of the Michaelis constant (Km) and the substrate concentration ([S]). By taking the inverse of V and [S], we can plot 1/V against 1/[S] and obtain a linear relationship. The slope of this line corresponds to 1/Vmax, and the y-intercept corresponds to 1/Km.