- The enzyme's absolute rigidity.
- Conformational changes in the enzyme upon substrate binding.
- The irreversible nature of catalysis.
- The enzyme's ability to act on multiple substrates.

Category: Biology etea medical mcqs
- Non-competitive inhibition.
- Competitive inhibition.
- Allosteric activation.
- Irreversible inhibition.
- A substrate molecule.
- A non-protein component.
- An active site.
- Specificity.
- Only peptide bonds.
- Covalent bonds between amino acids.
- Hydrogen bonds, ionic bonds, and disulfide bridges.
- Only hydrophobic interactions.
- The accumulation of the substrate of the deficient enzyme.
- The overproduction of the final product of the pathway.
- Increased activation energy for all metabolic reactions.
- Enhanced breakdown of all macromolecules.
- Maximum stability of the enzyme's primary structure.
- Efficient catalysis in its physiological setting.
- Irreversible denaturation under normal conditions.
- Its ability to bind to any substrate.
- The enzyme starts to break down.
- All active sites are continuously occupied by substrate molecules.
- The product inhibits the reaction.
- The temperature is too high.
- Permanently alters the enzyme's structure.
- Increases the energy of the products.
- Lowers the activation energy for the reaction.
- Prevents the release of products.
- They increase the cell's energy expenditure.
- They allow for efficient and continuous catalysis without constant synthesis.
- They make reactions irreversible.
- They reduce the need for substrate.
- A decrease in the enzyme's affinity for its substrate.
- An increase in the enzyme's turnover rate.
- A change in the active site's shape, reducing its catalytic efficiency.
- Direct competition with the substrate for binding.
- That the enzyme is being consumed.
- That the enzyme is undergoing denaturation.
- That the substrate is being used up.
- That the product is inhibiting the reaction.
- The reaction will not occur.
- The reaction will occur at a much slower rate.
- More product will be formed.
- The reaction will be irreversible.
- Increase metabolic rates.
- Permanently activate enzymes.
- Block the activity of specific disease-causing enzymes.
- Enhance substrate binding.
- Protein nature and complex tertiary structure.
- Ability to be reused multiple times.
- Sensitivity to temperature changes.
- Role as biological catalysts.
- Increasing temperature.
- Varying pH.
- Increasing substrate concentration.
- Changing enzyme concentration.
- The substrate concentration is very low.
- The temperature is below optimum.
- The substrate concentration is saturating.
- Product inhibition is occurring.
- A constantly changing structure regardless of substrate.
- A flexible structure that adapts upon substrate binding.
- Always perfectly complementary to the substrate.
- Only functional at optimal temperature.
- Its optimal pH.
- Its resistance to denaturation.
- The number of substrate molecules converted to product per unit time.
- Its molecular weight.
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