What type of interaction is NOT typically involved in the binding of substrates to enzymes?

The binding of substrates to enzymes primarily involves non-covalent interactions that facilitate the formation of the enzyme-substrate complex during the catalytic process. These interactions include hydrogen bonding, ionic bonding, and dipole-dipole interactions, as they allow substrates to fit into the active site of the enzyme without forming permanent chemical bonds.

Covalent bonding, on the other hand, involves the sharing of electrons between atoms to form a strong, stable bond. While some enzymes can transiently form covalent bonds with substrates during the catalytic cycle, this is not a typical mechanism for substrate binding. Enzymes usually rely on non-covalent interactions for the initial binding of the substrate, as these are generally more favorable for reversible binding and the dynamic nature of enzyme-substrate interactions. Therefore, covalent bonding is not typically involved in the primary binding interactions with substrates.