What is the Difference Between Allosteric and Non-allosteric Enzymes?
🆚 Go to Comparative Table 🆚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:
Feature | Allosteric Enzymes | Non-allosteric Enzymes |
---|---|---|
Definition | Enzymes with an additional regulatory site called allosteric site. | Enzymes with only an active site for binding the substrate. |
Active Sites | Multiple active sites located on different protein subunits. | Single active site. |
Regulation | Regulated by allosteric inhibitors or activators that bind to the allosteric site. | Not regulated by allosteric inhibitors or activators. |
Substrate Specificity | Substrate-specific enzymes. | Substrate-specific enzymes. |
Reaction Rate | Reaction rate changes when an allosteric inhibitor or activator binds. | Reaction rate is not affected by allosteric inhibitors or activators. |
Examples | Aspartate transcarbamoylase and ADP-glucose pyrophosphorylase. | Specific examples not provided in the search results. |
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.
- Non-Competitive vs Allosteric Inhibition
- Allosteric Site vs Active Site
- Enzymatic vs Nonenzymatic Reaction
- Allozymes vs Isozymes
- Allosteric vs Covalent Modulation
- Enzyme vs Coenzyme
- Enzyme vs Hormone
- Catalyst vs Enzyme
- Anabolic vs Catabolic Enzymes
- Enzyme Inhibitor vs Enzyme Inducer
- Exoenzyme vs Endoenzyme
- Enzyme Activator vs Enzyme Inhibitor
- Positive vs Negative Allosterism
- Enzyme Activity vs Specific Activity
- Enzyme vs Protein
- Competitive vs Noncompetitive Inhibition
- Allozyme Isozyme vs Isoform
- Isomerase vs Mutase Enzyme
- Catalytic vs Non Catalytic Reaction