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Multiple Choice
In a Michaelis-Menten kinetics plot (V0 vs. [S]), what is the reason that the curve reaches a plateau and V0 cannot increase any further upon adding more substrate?
A
The enzyme becomes locked in an inactive conformation.
B
Enzymes match rate of catalysis & rate of ES formation.
C
The active site of all the enzymes are saturated with substrate.
D
There is an inhibitor present.
E
Vmax can only be attained by some enzymes.
F
Enzyme is locked in an inactive conformation.
Verified step by step guidance
1
Understand the concept of Michaelis-Menten kinetics: This model describes the rate of enzymatic reactions by relating reaction rate (V0) to substrate concentration ([S]). The key parameters are Vmax (maximum rate) and Km (Michaelis constant).
Recognize the significance of Vmax: Vmax represents the maximum rate of the reaction when the enzyme is saturated with substrate. It is the plateau observed in the Michaelis-Menten plot.
Identify the reason for the plateau: The plateau occurs because all active sites of the enzyme molecules are occupied by substrate, meaning the enzyme is working at its maximum capacity.
Consider the role of substrate concentration: As substrate concentration increases, the reaction rate increases until all enzyme active sites are occupied. Beyond this point, adding more substrate does not increase the rate further.
Clarify the concept of enzyme saturation: Enzyme saturation means that every enzyme molecule is bound to a substrate molecule, and the reaction rate is at its maximum (Vmax). This is why the curve reaches a plateau in the plot.