What is the next step in the process after a substrate enters the active site of an enzyme?

When a substrate enters the active site of an enzyme, several key steps follow in the enzymatic reaction process:

1. Formation of the Enzyme-Substrate Complex: The substrate binds to the active site of the enzyme, forming a transient enzyme-substrate complex (ES complex). This binding typically involves multiple non-covalent interactions such as hydrogen bonds, ionic bonds, and hydrophobic interactions.

2. Induced Fit: Once the substrate is bound, the enzyme may undergo a conformational change to better accommodate the substrate. This "induced fit" enhances the ability of the enzyme to catalyze the reaction.

3. Catalysis: The enzyme catalyzes the conversion of the substrate into products by lowering the activation energy required for the reaction to occur. This may involve temporary changes in the substrate's chemical bonds, typically resulting in the formation of products.

4. Release of Products: After the reaction, the newly formed products have a lower affinity for the active site compared to the substrate. Thus, they are released from the enzyme, allowing the enzyme to return to its original state and become available to catalyze another reaction.

This sequence of events highlights the specific and dynamic nature of enzyme-substrate interactions, crucial for facilitating biochemical reactions within the cell.