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When an enzyme is denatured, it loses its specific three-dimensional shape, rendering it unable to perform its biological function.
Enzymes are biological catalysts that speed up chemical reactions in living organisms. They are proteins with a specific three-dimensional shape, which is crucial for their function. This shape is determined by the sequence of amino acids in the protein, and it forms a specific active site where the substrate molecules bind.
Denaturation is a process that alters the enzyme's structure without breaking the peptide bonds that hold the amino acids together. This can be caused by changes in temperature, pH, or exposure to certain chemicals. When an enzyme is denatured, its active site changes shape or even disappears, meaning the substrate can no longer fit into it. This renders the enzyme inactive as it can no longer catalyse reactions.
For example, if you heat an enzyme beyond its optimum temperature, the increased kinetic energy causes the enzyme's molecules to vibrate more. This can break the hydrogen bonds holding the enzyme in shape, leading to denaturation. Similarly, changes in pH can affect the charges on the amino acid residues at the active site, disrupting the interactions that hold the enzyme in shape.
It's important to note that denaturation is usually irreversible. Once an enzyme has been denatured, it's often impossible for it to return to its original shape and regain its function. This is why maintaining stable conditions in the body is so crucial; if the body's temperature or pH levels fluctuate too much, it can lead to enzyme denaturation and disrupt normal bodily functions.
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