This may help a little. Although this may appear to be all about temperature, read thourough it and note that temperature denatures the enzyme and how that affects the K and the Arrhenius equation.
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An enzyme gets denatured at high temperatures and if the environment is too acidic or basic. Some enzymes work better in certain conditions but extreme conditions denature all proteins. What happens is that the bonds and links between the amino acids that make up the protein are broken and the protein unfolds and denatures. In other words, it stops working. It loses its conformation.
Hope that helps.
What is the connection between denaturation and the enzyme activity, on a chemical level?
Also, what does it have to do with the lock and key model of enzyme action?
I understand the basic definitions of denaturation, enzyme activity, and lock and key model, but I just can't seem to string them together.
Thank you so much and Merry Christmas!
The connection between denaturation and enzyme activity on a chemical level is that denaturation leads to the loss of the enzyme's active conformation, which is necessary for the enzyme to carry out its specific biochemical reactions. When an enzyme is denatured, its structure is disrupted, resulting in the loss or alteration of its active site. The active site is a specific region of the enzyme where the substrate molecule binds and undergoes a chemical reaction.
In the lock and key model of enzyme action, the enzyme's active site is often compared to a lock and the substrate molecule as the key. Just as a lock can only be opened by a specific key, an enzyme can only bind to and catalyze a specific substrate molecule. The lock and key model emphasizes the specificity of enzyme-substrate interactions, meaning that an enzyme can only interact with its specific substrate due to the complementary shape of their molecular structures.
However, with denaturation, the enzyme's active site can become distorted or unfolded, disrupting the necessary shape and structure for the lock and key interaction. This leads to a loss of specificity in substrate binding, resulting in decreased or complete loss of enzymatic activity. Essentially, denaturation causes the lock to lose its shape, making it incompatible with the key.
In summary, denaturation disrupts the enzyme's active conformation, which affects the enzyme's ability to interact with its substrate. This connection is related to the lock and key model as denaturation alters the shape of the active site, rendering it unable to recognize and bind to the specific substrate, just like a misshaped lock unable to be opened by the correct key.