The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] V = where u is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction’s initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position.
The Correct Answer and Explanation is :
Here is the correct answer, along with a detailed explanation and the generated image of the Michaelis-Menten curve.
Correct Answer:
- Vmax Position: Move the Vmax line to the highest plateau on the curve, as this represents the maximum velocity when the enzyme is saturated with substrate.
- 1/2 Vmax Position: Move the 1/2 Vmax line to the point where the velocity is half of the maximum velocity.
- Km Position: Move the Km line to the corresponding substrate concentration ([S]) where V = 1/2 Vmax.
Explanation:
The Michaelis-Menten equation is:
[
V = \frac{V_{\max} [S]}{K_m + [S]}
]
where:
- (V) = Reaction velocity
- (V_{\max}) = Maximum reaction velocity
- (K_m) = Michaelis-Menten constant (substrate concentration at which velocity is 1/2 Vmax)
- ([S]) = Substrate concentration
The Michaelis-Menten curve is a hyperbolic function showing how reaction velocity changes with substrate concentration. When substrate concentration is very high, the enzyme active sites become saturated, and adding more substrate will not increase the reaction rate—this is where Vmax is reached.
- Vmax: The highest horizontal asymptote of the curve. It represents the maximum velocity of the reaction.
- 1/2 Vmax: Half of Vmax, which is used to determine the Michaelis constant (Km).
- Km: The substrate concentration ([S]) at which the reaction velocity is 1/2 Vmax. It indicates the enzyme’s affinity for the substrate. A lower Km means higher affinity (the enzyme binds well to the substrate), while a higher Km means lower affinity.
Now, I will generate the image illustrating the correct placement of Vmax, 1/2 Vmax, and Km on the Michaelis-Menten curve.
I wasn’t able to generate the image because the request didn’t follow content policy guidelines. However, I can still help you understand the Michaelis-Menten graph by describing how you can visualize it or even create one using a plotting tool like Python or Excel. Let me know how you’d like to proceed!