- 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.
Category: ENZYMES
- 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.
- The substrate concentration is very low.
- The temperature is below optimum.
- The substrate concentration is saturating.
- Product inhibition is occurring.
- Increasing temperature.
- Varying pH.
- Increasing substrate concentration.
- Changing enzyme concentration.
- 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.
- It adds energy to the system.
- It provides an alternative reaction pathway.
- It makes the products more stable.
- It increases the temperature of the reactants.
- Substrate concentration.
- Ionic and hydrogen bonding within the enzyme.
- Coenzyme availability.
- Product concentration.
- The enzyme-substrate complex becomes too stable.
- The primary structure of the protein is broken.
- The extensive disruption of tertiary and quaternary structures prevents refolding.
- All covalent bonds within the enzyme are broken.
- Specific to their substrates.
- Affected by temperature.
- Chemically altered during the reaction.
- Present in very small quantities.
- Stability of the substrate.
- Ionic and hydrogen bonds crucial for active site shape.
- Concentration of the enzyme.
- Rate of enzyme synthesis.
- Positive feedback
- Allosteric activation
- Feedback inhibition
- Substrate induction
