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The Michaelis-Menten equation is an expression of the relationship between the initial velocity,V0, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation to an expression from which the effect of [S] on the rate can be more readily determined.

- Match the condition (there are 6 total) (e.g. [S] = Km) with the statement(s) that describe it.
- Doubling [S] will almost double the rate.
- Half of the active sites are occupied by substrate.
- About 90% of the active sites are occupied by substrate.
- Doubling [S] will have little effect on the rate.
- Less than 10% of the active sites are occupied by substrate.
- This condition will result in the highest rate.
- The three conditions to choose/match from are [S]=0.1 Km, [S]=Km, and [S]=10 Km

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Final answer:

The Michaelis-Menten equation describes the relationship between the initial velocity (V0) of an enzymatic reaction and the substrate concentration ([S]). To simplify the equation and determine the effect of [S] on the rate more easily, three conditions can be matched: [S] = 0.1 Km, [S] = Km, and [S] = 10 Km.

Step-by-step explanation:

The Michaelis-Menten equation describes the relationship between the initial velocity (V0) of an enzymatic reaction and the substrate concentration ([S]). To simplify the equation and determine the effect of [S] on the rate more easily, three conditions can be matched:

  1. [S] = 0.1 Km: Doubling [S] will almost double the rate.
  2. [S] = Km: Half of the active sites are occupied by substrate.
  3. [S] = 10 Km: About 90% of the active sites are occupied by substrate. This condition will result in the highest rate.
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