What's the effects of substrate concentration for enzymes?
The effects of substrate concentration on enzyme activity can be summarized as follows:
1. Low substrate concentration: At low substrate concentrations, the enzyme will have fewer substrate molecules to bind to, leading to a slower rate of reaction. Once all available enzyme active sites are filled with substrate molecules, further increase in substrate concentration will not increase the rate of reaction.
2. Optimal substrate concentration: At the optimal substrate concentration, the enzyme active sites are saturated with substrate molecules, leading to the maximum rate of reaction. This is known as the Vmax of the enzyme.
3. High substrate concentration: At high substrate concentrations, the enzyme active sites are saturated with substrate molecules and cannot bind to any more. This leads to a plateau in the reaction rate, as the enzyme is working at its maximum capacity. Further increase in substrate concentration will not increase the rate of reaction.
In conclusion, the rate of enzyme activity is directly proportional to the substrate concentration up to a certain point, after which it reaches a plateau. This relationship is represented by the Michaelis-Menten curve.