What is the Difference Between Allosteric and Non-allosteric Enzymes?

The main difference between allosteric and non-allosteric enzymes lies in the presence of an additional regulatory site called the allosteric site in allosteric enzymes, while non-allosteric enzymes have only an active site for binding the substrate. Here are the key differences between allosteric and non-allosteric enzymes:

• Allosteric Enzymes:
• Have both an active site and an allosteric site.
• Are regulatory enzymes, meaning they can be regulated by molecules binding to the allosteric site.
• Can be affected by allosteric inhibitors or activators, which bind to the allosteric site and either decrease or increase the enzyme's activity.
• Exhibit cooperativity, where the binding of a molecule at one active site can affect the activity of other active sites on the protein subunits.
• Non-allosteric Enzymes:
• Have only an active site for binding the substrate.
• Are not regulatory enzymes, as they lack an allosteric site.
• Are substrate-specific, while allosteric enzymes are both substrate and regulatory molecule specific.

In summary, allosteric enzymes have an additional allosteric site that can be used for regulation, while non-allosteric enzymes only have an active site for substrate binding.

Comparative Table: Allosteric vs Non-allosteric Enzymes

Allosteric and non-allosteric enzymes are two types of enzymes that differ in their structure and regulation. Here is a table highlighting the differences between them:

Both allosteric and non-allosteric enzymes are made up of proteins, catalyze biochemical reactions in living cells, remain unchanged at the end of the reaction, and are sensitive to changes in pH and temperature.