Answer:
The state in which all active sites of an enzyme are occupied and no more substrate molecules can find a free active site is called enzyme saturation or substrate saturation.
Enzyme saturation occurs when the concentration of substrate molecules is so high that all available active sites on the enzyme molecules are already bound to substrate molecules. At this point, increasing the concentration of substrate will not lead to an increase in the rate of the reaction because all the enzyme molecules are already engaged in the catalytic process.
This state can be visualized with the analogy of a crowded room. If there are only a few people in the room (low substrate concentration), there are plenty of empty seats (active sites) for newcomers (substrate molecules) to occupy. However, as more people enter the room (increased substrate concentration), eventually all the seats (active sites) become occupied, and newcomers (substrate molecules) cannot find an empty seat (free active site).
Enzyme saturation is an important concept in enzyme kinetics, as it determines the maximum rate of a reaction (Vmax). At this point, increasing the substrate concentration further will not increase the reaction rate, as the enzyme is already working at its maximum capacity.
Step-by-step explanation: