What is the Difference Between Allosteric Site and Active Site?

The main difference between an allosteric site and an active site lies in their functions and locations within an enzyme:

• Allosteric Site:
• An allosteric site is a regulatory site on a protein that can affect its activity.
• It is distinct from the active site and is not involved in the catalytic reaction.
• Allosteric sites can be influenced by activator or inhibitor molecules, which can bind to the enzyme to either increase or decrease its activity.
• Allosteric sites are present only in allosteric enzymes.
• Active Site:
• The active site is where a substrate binds and the catalytic reaction occurs.
• It is the region of an enzyme where substrate molecules bind and catalyze the reaction.
• Active sites are present in all enzymes.

In summary, an allosteric site is a regulatory site on an enzyme that can be influenced by activator or inhibitor molecules, while an active site is the region where substrate molecules bind and the catalytic reaction occurs. Both sites play crucial roles in enzyme activity and enzyme-catalyzed reactions.

Comparative Table: Allosteric Site vs Active Site

Here is a table summarizing the differences between allosteric sites and active sites:

In summary, allosteric sites are regulatory sites on proteins that can affect their activity, while active sites are where substrate molecules bind and chemical reactions occur. Allosteric sites can be affected by environmental factors and can either increase or decrease enzyme activity, while active sites are part of the enzyme's structure and catalyze reactions without changing the enzyme's structure.