Enzymes bind to substrates through which specific feature in the active site?

Enzymes primarily bind to substrates through amino acids located in the active site. The active site of an enzyme is a specific region where the substrate molecule fits, allowing for a reaction to occur. The binding is facilitated through various interactions, such as hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals forces, which are largely dependent on the side chains of the amino acids present in the active site.

Each enzyme has a unique active site shaped to accommodate its specific substrate, and alterations in the amino acid composition can significantly affect the enzyme's ability to function. This specificity is crucial for catalytic efficiency and selectivity. In contrast, carbohydrates, nucleotides, and fatty acids do not play a direct role in the substrate binding mechanism in the manner that amino acids do, as they are not components of the active site's structure responsible for substrate interaction. Thus, the role of amino acids in forming the active site's remainder is fundamental to enzyme activity.