Question

Draw a graph showing how substrate concentration affects the initial rate of an enzyme-controlled reaction

Answer 1

The graph portraying substrate concentration's effect on an enzyme-controlled reaction's initial rate shows a steep rise followed by a plateau, signifying the direct impact of substrate concentration until enzyme saturation occurs.

Step-by-step explanation:

The initial rate of an enzyme-controlled reaction is affected by the substrate concentration. Initially, as the substrate concentration
`(_[S]_)`increases, the rate of the reaction
`(_v0_)` also rises steeply due to more frequent collisions between the substrate and the enzyme's active site. This increased collision frequency leads to more enzyme-substrate complexes formed and, consequently, more product formation per unit time.

`\[ \text{Rate} = k * [\text{Enzyme}] * [\text{Substrate}] \]`

Where _k_ is the rate constant, [\text{Enzyme}] is the enzyme concentration (assumed constant), and [Substrate] is the substrate concentration. However, as the substrate concentration continues to increase, the enzyme's active sites become increasingly saturated
`(_[ES]_ reaches a maximum)`, resulting in a plateau in the reaction rate. At this point, adding more substrate doesn't significantly increase the rate, as the enzyme is working at its maximum capacity.

This behavior is represented by a hyperbolic curve on the graph plotting the initial rate against substrate concentration. The curve rises steeply at low substrate concentrations, indicating the enzyme's efficiency, and then levels off, showing saturation. Understanding this relationship is crucial in determining optimal conditions for enzyme-controlled reactions.