When reviewing a Michaelis-Menten Saturation Curve, at first the rate of the reaction is relatively constant, but the rate decreases as the substrate is used up and eventually reaches a plateau. reaching this plateau, what would speed up the reaction again? Adding more substrate Adding heat Adding more enzyme Adding cofactors

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**Understanding the Michaelis-Menten Saturation Curve**

When reviewing a Michaelis-Menten Saturation Curve, initially, the rate of the reaction is relatively constant. However, as the substrate is used up, the rate decreases and eventually reaches a plateau. This plateau represents the maximum reaction rate achieved with the available enzyme. 

**Question:**

After reaching this plateau, what action would speed up the reaction again?

1. Adding more substrate
2. Adding heat
3. Adding more enzyme
4. Adding cofactors

**Explanation:**

In the context of enzyme kinetics, the plateau occurs because all enzyme active sites are saturated with substrate. To increase the reaction rate after reaching this point, adding more enzyme would be effective, as it provides more active sites for substrate molecules to bind, allowing for an increased overall reaction rate. 

Other options like adding more substrate will not affect the rate once saturation is achieved; adding heat may increase the rate but risks denaturing the enzyme, while adding cofactors aids enzyme activity only if the enzyme is deficient in its cofactors.
Transcribed Image Text:**Understanding the Michaelis-Menten Saturation Curve** When reviewing a Michaelis-Menten Saturation Curve, initially, the rate of the reaction is relatively constant. However, as the substrate is used up, the rate decreases and eventually reaches a plateau. This plateau represents the maximum reaction rate achieved with the available enzyme. **Question:** After reaching this plateau, what action would speed up the reaction again? 1. Adding more substrate 2. Adding heat 3. Adding more enzyme 4. Adding cofactors **Explanation:** In the context of enzyme kinetics, the plateau occurs because all enzyme active sites are saturated with substrate. To increase the reaction rate after reaching this point, adding more enzyme would be effective, as it provides more active sites for substrate molecules to bind, allowing for an increased overall reaction rate. Other options like adding more substrate will not affect the rate once saturation is achieved; adding heat may increase the rate but risks denaturing the enzyme, while adding cofactors aids enzyme activity only if the enzyme is deficient in its cofactors.
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