How do enzymes interact with substrates to form products?

Enzymes interact with substrates by binding to them at the active site, facilitating a chemical reaction to form products.

Enzymes are biological catalysts that speed up chemical reactions in living organisms. They are proteins with a specific three-dimensional structure, which includes an area known as the active site. The active site is where the substrate, the molecule upon which the enzyme acts, binds. This binding is often likened to a 'lock and key' model, where the enzyme (the lock) has a specific shape that perfectly fits the substrate (the key).

The interaction between the enzyme and substrate is not passive. When the substrate binds to the enzyme's active site, it forms an enzyme-substrate complex. This binding induces a change in the enzyme's shape, a process known as induced fit. This change in shape stresses the bonds in the substrate, lowering the activation energy required for the reaction to occur. The enzyme then catalyses the reaction, converting the substrate into the product.

The enzyme remains unchanged after the reaction and can be used again to catalyse the same reaction with another substrate molecule. This is why enzymes are so efficient and can facilitate thousands of reactions per second.

The specificity of enzymes is also crucial. Each enzyme is designed to catalyse a specific reaction or a group of closely related reactions. This specificity is determined by the unique shape and structure of the enzyme's active site, which is complementary to the shape of its substrate. This ensures that the enzyme only interacts with the correct substrate, leading to the formation of the desired product.

In summary, enzymes interact with substrates by binding to them at their active site, undergoing an induced fit, and catalysing a chemical reaction to form products. This process is highly efficient and specific, making enzymes vital for life's biochemical processes.