The three-dimensional structure of a functional protein is altered by intense heat or nonphysiological ph even though peptide bonds may not break. such inactivation is called denaturation, and denatured enzymes are nonfunctional. explain why.

In biochemistry, enzymes are protein catalysts of the body that speeds up certain specific metabolic reactions in the body. They word in the concept of lock-and-key theory or induced fitting. These two theories are all based on the shape and size of the enzyme's active site that could accommodate the substrate. So, the main function of the enzyme is dependent on its shape. Therefore, when an enzyme undergoes denaturation, its orientation and shape changes. For example, a beta pleated sheet may change to an alpha helix orientation. As a consequence, the number and capacity of active sites changes. Hence, the enzyme becomes nonfunctional.