Upon non-covalent association of an enzyme to its substrate, a loss in entropy of motion occurs. In other words, some translational and rotational degrees of freedom are lost. As a result,
It has been seen that the interaction between the active site and the substrate involves non-covalent interactions like hydrogen bonds, Vanderwalls interactions, hydrophobic interactions and electrostatic interactions. These interactions are transient and the substrate is held in proper orientation. These interactions facilitate the formation of E-S complex (Enzyme substrate complex) for catalyzing the forward biochemical reaction leading to the synthesis of product.
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