- The enzyme is irreversibly denatured.
- The product is released from the enzyme.
- The substrate is correctly positioned for catalysis.
- The activation energy is increased.
Category: ENZYMES
- 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.
- End product molecules.
- Cofactor molecule.
- Transition state of the substrate.
- Inhibitor molecule.
- Km? (Michaelis constant)
- Vmax? (maximum velocity)
- Substrate concentration
- Activation energy
- 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.
- Catalyze irreversible reactions.
- Bind to a wider range of substrates.
- Adapt their shape slightly to better fit the substrate.
- Function without a specific active site.
- How many times it can be reused.
- The rate at which it denatures.
- How many substrate molecules it can convert per unit time.
- Its sensitivity to pH.
- The enzyme is being denatured by excess substrate.
- The reaction reaches equilibrium.
- All enzyme active sites become occupied.
- Product accumulation inhibits the reaction.
- Availability of cofactors.
- Concentration of enzyme molecules.
- Number of active sites available for substrate binding.
- Optimal pH of the reaction.
- Reversible competitive inhibitor
- Irreversible inhibitor
- Allosteric activator
- Non-competitive allosteric activator
- Isomerase
- Hydrolase
- Ligase
- Lyase
- Reusability
- Specificity
- Temperature optimum
- pH optimum
- Cause denaturation.
- Slow down molecular motion.
- Irreversibly alter the active site.
- Increase activation energy.
- Ability to bind to an allosteric site.
- Tendency to form temporary bonds with the enzyme.
- Structural similarity to the substrate.
- Effect on the enzyme's Vmax?.
- Cofactor molecule
- Inhibitor molecule
- Substrate molecule
- Product molecule
- Increasing overall product yield.
- Maintaining cellular energy balance.
- Preventing wasteful overproduction of substances.
- Accelerating the metabolic pathway.
- Becomes rigid upon substrate binding.
- Changes shape slightly to better accommodate the substrate.
- Can bind to any molecule.
- Is identical for all enzymes.
