What is the Difference Between Positive and Negative Allosterism?

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The difference between positive and negative allosterism lies in the effect that the binding of an effector molecule has on the enzyme's activity and configuration.

  • Positive Allosterism: In this case, the binding of an effector molecule to an enzyme causes the enzyme to change into its active configuration, leading to an increase in the enzyme's activity. Positive allosterism in proteins shows a high affinity for ligands.
  • Negative Allosterism: In this case, the binding of an effector molecule to an enzyme causes the enzyme to change into its inactive configuration, leading to a decrease in the enzyme's activity. Negative allosterism in proteins shows a low affinity for ligands.

In summary, positive allosterism activates the enzyme and increases its activity, while negative allosterism inhibits the enzyme and decreases its activity.

Comparative Table: Positive vs Negative Allosterism

The difference between positive and negative allosterism lies in the effect of the binding of an effector molecule to a protein, such as an enzyme. Here is a comparison table highlighting the key differences:

Feature Positive Allosterism Negative Allosterism
Affinity for Ligands High affinity for ligands Low affinity for ligands
Effect on Enzyme Activity Increases enzyme activity Decreases enzyme activity
Conformational Change Enzyme changes into its active configuration Enzyme changes into its inactive configuration
Type of Interaction Allosteric Activation Allosteric Inhibition
Example Oxygen-hemoglobin interaction (Positive cooperativity) Binding of an allosteric inhibitor to an enzyme, causing a conformational change that decreases its affinity for the substrate

Positive allosterism is characterized by a high affinity for ligands and results in an increase in enzyme activity, while negative allosterism is characterized by a low affinity for ligands and results in a decrease in enzyme activity.