What is the Difference Between Holoenzyme and Apoenzyme?
🆚 Go to Comparative Table 🆚The main difference between holoenzyme and apoenzyme lies in their catalytic activity and the presence of a cofactor:
- Holoenzyme: This is the catalytically active form of an enzyme, which includes both the apoenzyme and the cofactor. The holoenzyme is fully functional and can catalyze biochemical reactions.
- Apoenzyme: This is the catalytically inactive protein component of the enzyme. The apoenzyme becomes active only after attaching to a cofactor, forming a holoenzyme.
A summary of the differences between holoenzyme and apoenzyme can be presented in the following table:
| Holoenzyme | Apoenzyme |
|---|---|
| Catalytically active | Catalytically inactive |
| Contains protein and cofactor(s) | Contains only protein |
| Fully functional to catalyze biochemical reactions | Inactive and becomes active only after attaching to a cofactor |
| Examples: DNA polymerase, RNA polymerase, carbonic anhydrase | Examples: carbonic anhydrase without Zn2+ ions |
Cofactors can be metal ions (e.g., Mg2+, Fe3+, Zn2+), organic molecules or coenzymes (e.g., NAD+, NADP+, FAD2+), and prosthetic groups.
On this pageWhat is the Difference Between Holoenzyme and Apoenzyme? Comparative Table: Holoenzyme vs Apoenzyme
Comparative Table: Holoenzyme vs Apoenzyme
Here is a table summarizing the differences between holoenzymes and apoenzymes:
| Feature | Holoenzyme | Apoenzyme |
|---|---|---|
| Definition | Holoenzymes are catalytically active enzymes that consist of a protein and a non-protein part (cofactor) essential for their activity. | Apoenzymes are the inactive protein components of enzymes that become active only after attaching to a cofactor. |
| Activity | Holoenzymes are catalytically active, meaning they can initiate and catalyze biochemical reactions. | Apoenzymes are catalytically inactive and cannot initiate reactions without attaching to a cofactor. |
| Completeness | Holoenzymes are complete and can initiate the reaction without the need for additional components. | Apoenzymes are incomplete without their cofactors and will not initiate reactions. |
| Examples | DNA polymerase, RNA polymerase, lactase, hexokinase, and DNA ligase are examples of holoenzymes. | Aspartate transcarbamoylase is an example of an apoenzyme. |
In summary, holoenzymes are active enzyme-cofactor complexes, while apoenzymes are inactive protein components that require a cofactor to become active and initiate catalytic function.
Read more:
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- Enzyme vs Protein
- Catalyst vs Enzyme
- RNA Polymerase Core vs Holoenzyme
- Isomerase vs Mutase Enzyme
- Protease vs Proteinase
- Proteasome vs Protease
- Proteolytic Enzymes vs Digestive Enzymes
- Protease vs Peptidase
- Allozyme Isozyme vs Isoform
- Anabolic vs Catabolic Enzymes
- Metalloenzymes vs Metal Activated Enzymes
- Homolysis vs Heterolysis
- Acid Hydrolysis vs Enzymatic Hydrolysis
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