Non-competitive inhibition often results in

Options

A. Change in enzyme structure
B. Blocking of active site
C. Non-synthesis of enzymes
D. Non-aviaility of cofactore.

Answer

### Step-by-Step Solution:

1. **Understanding Non-Competitive Inhibition**: Non-competitive inhibition occurs when an inhibitor binds to an enzyme at a site other than the active site. This binding changes the enzyme's shape, preventing the substrate from binding effectively.

2. **Enzyme Structure**: Enzymes have specific shapes that allow substrates to fit into their active sites. In non-competitive inhibition, the inhibitor binds to a different site on the enzyme, known as the allosteric site.

3. **Effect of Inhibitor Binding**: When the inhibitor binds to the allosteric site, it alters the enzyme's conformation (shape). This change in structure means that even if the substrate is present, it cannot bind to the active site properly.

4. **Resulting Impact on Enzyme Activity**: Non-competitive inhibition decreases the overall number of active enzyme molecules available for catalysis, leading to a reduction in the maximum rate of reaction (Vmax). However, it does not affect the affinity of the enzyme for the substrate (Km remains unchanged).

5. **Conclusion**: Therefore, non-competitive inhibition often results in a decrease in the maximum rate of reaction without affecting the binding affinity of the enzyme for the substrate.