Inhibition Enzyme kinetics

Competitive inhibition
1. Inhibitors are structurally similar to the substrate
2. Inhibitors compete with substrate for the active site
3. The inhibition effect can overcome by increase the concentration of substrate
4. Vmax remain the same and Km increase. This is because increase the concentration of substrate will decrease the chance of the inhibitor to bind to the active site. Therefore, the Km will be higher because higher concentration of substrate is required.
Non competitive inhibition
1. Inhibitors are not struturally similar to substrate.
2. Inhibitors are not bind to active site, but bind to allosteric site.
3. The conformation shape of active site will altered once inhibitor bind to the allosteric site which cause the substate no longer able to bind to active site.
4. Vmax decrease and Km remain the same. This is because the inhibition cannot overcome by increasing the concentration of substrate. Therefore, the production of products will decrease which leads to the decrease in Vmax and nothing change in Km.
Uncompetitive inhibition
1. Inhibitors are not structurally similar to the substrate.
2. Inhibitors bind to a site on the enzyme when enzyme-substrate complex is formed.
3. The binding of the inhibitors prevent the production of the products.
4. Vmax and Km both decrease. This is because increase in concentration of substrate won't help in overcome the inhibition which leads to the decrease in Vmax. The binding of the inhibitor enhances the binding of substrate which leads to the reducing in Km.
Vmax is reached when all the enzymes are saturated with substrate.
Small Km means the enzyme requires small amount of substrate to become saturated. Large Km means the enzyme requires large amount of substrate to become saturated.

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Inhibition Enzyme kinetics

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	Created by Ee Lyn Yap over 8 years ago