What is the Relationship Between Km and V0 in the Michaelis-Menten Curve?

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  • Thread starter TytoAlba95
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In summary, the Michaelis-Menten curve shows that in the region where [S] is less than Km, doubling [S] will approximately double the reaction velocity. However, in the region where [S] is greater than Km, the reaction velocity will not double as the slope decreases and the rise of V0 with S will be less than double.
  • #1
TytoAlba95
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Homework Statement
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Relevant Equations
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The relevant formua: V0= (Vmax x )/ (Km + )
From the question:
2(Vmax x 0.5)/ (Km + 0.5) = (Vmax x 1)/ (Km + 1)
=> 2(Vmax x 0.5)/ (Km + 0.5) = (Vmax x 1)/ (Km + 1)
=> 1 x (Km +1) = (Km + 0.5)

Where am I making the mistake?
 
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  • #2
This is a conceptual question that does not require any calculations to solve. Consider the shape of a general Michaelis-Menten curve (it may be helpful to draw one). In the region where [ S] < Km, if you double [ S] will the reaction velocity approximately double? In the region where [S] > Km, if you double [ S] will the reaction velocity approximately double?
 
  • #3
Considering the general Michaelis-Menten curve, in the region where S < Km, the V0- relationship is linear, so yes the reaction velocity doubles as S approximately doubles.
It is not the same when S > Km, because the slope decreases, the rise of V0 with S will be less than double.
 
  • #4
TytoAlba95 said:
Considering the general Michaelis-Menten curve, in the region where S < Km, the V0- relationship is linear, so yes the reaction velocity doubles as S approximately doubles.
It is not the same when S > Km, because the slope decreases, the rise of V0 with S will be less than double.

Yes, that is correct. With these principles in mind, this should lead you to the correct response.
 

Related to What is the Relationship Between Km and V0 in the Michaelis-Menten Curve?

1. What is the Km value of an enzyme?

The Km value of an enzyme is the substrate concentration at which the enzyme works at half of its maximum velocity. It is a measure of the affinity of the enzyme for its substrate.

2. How is the Km value determined?

The Km value is determined by plotting the initial reaction rate against different substrate concentrations and finding the concentration at which the reaction rate is half of the maximum rate. This is known as the Michaelis-Menten plot.

3. What does a low Km value indicate about an enzyme?

A low Km value indicates that the enzyme has a high affinity for its substrate, meaning that it can efficiently catalyze the reaction even at low substrate concentrations. This also means that the enzyme is more active and requires less substrate to reach its maximum velocity.

4. How does temperature affect the Km value of an enzyme?

Temperature can affect the Km value of an enzyme by altering its shape and therefore its affinity for the substrate. Generally, an increase in temperature can decrease the Km value, making the enzyme more active and efficient.

5. Can the Km value of an enzyme change?

Yes, the Km value of an enzyme can change under different conditions such as temperature, pH, and the presence of inhibitors. Changes in the enzyme's structure can also alter its Km value. Additionally, different enzymes can have different Km values for the same substrate.

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