- Increase metabolic rates.
- Permanently activate enzymes.
- Block the activity of specific disease-causing enzymes.
- Enhance substrate binding.
No category found.
- 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.
- Substrate concentration.
- Ionic and hydrogen bonding within the enzyme.
- Coenzyme availability.
- Product concentration.
- 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.
- 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.
- Positive feedback
- Allosteric activation
- Feedback inhibition
- Substrate induction
- Stability of the substrate.
- Ionic and hydrogen bonds crucial for active site shape.
- Concentration of the enzyme.
- Rate of enzyme synthesis.
- The enzyme is irreversibly denatured.
- The product is released from the enzyme.
- The substrate is correctly positioned for catalysis.
- The activation energy is increased.
- Decreasing the temperature.
- Increasing the enzyme concentration.
- Increasing the substrate concentration.
- Altering the pH to be acidic.
- A higher yield of product.
- A faster rate of reaction.
- A change in the equilibrium point.
- A greater energy release from the reaction.
- Km? (Michaelis constant)
- Vmax? (maximum velocity)
- Substrate concentration
- Activation energy
- End product molecules.
- Cofactor molecule.
- Transition state of the substrate.
- Inhibitor molecule.
- Substrate molecules become limiting.
- The enzyme's kinetic energy decreases.
- The enzyme undergoes conformational changes that reduce its catalytic efficiency.
- Product inhibition becomes dominant.
- Prevents substrate binding.
- Alters the overall 3D folding and thus the active site's shape.
- Increases the enzyme's affinity for its product.
- Makes the enzyme more resistant to denaturation.
