- Allosteric activation
- Feedforward activation
- Feedback inhibition
- Competitive activation
Author: ETEA MCQS.COM
No category found.
- Sensitivity to temperature
- Specificity to substrate
- Reversibility
- Allosteric regulation
- Increased enzyme stability
- Enhanced catalytic efficiency
- Reduced or lost enzyme activity
- A change in optimal pH
- Generate heat during reaction
- Lower the activation energy barrier
- Increase the concentration of reactants
- Shift the reaction equilibrium significantly
- Allosteric site
- Regulatory site
- Active site
- Cofactor binding site
- Increased kinetic energy of substrate
- Enzyme saturation
- Denaturation of the enzyme protein
- Increased product concentration
- Competitive inhibitor
- Allosteric activator
- Non-competitive inhibitor
- Substrate analogue
- Each enzyme can catalyze any type of reaction.
- An enzyme will only bind to certain types of cofactors.
- Each enzyme typically catalyzes only one or a few related reactions.
- Enzymes are only found in specific cells.
- Free energy
- Binding energy
- Kinetic energy
- Activation energy
- A temporary slowdown in reaction rate
- Complete and lasting inactivation of the enzyme
- Increased enzyme affinity for substrate
- Reversible conformational changes
- Bind to an allosteric site
- Form an irreversible bond with the enzyme
- Bind to the active site of the enzyme
- Increase the activation energy of the reaction
- Inhibit the enzyme's action
- Alter the pH of the reaction
- Enhance catalytic activity by assisting in substrate binding or catalysis
- Denature the enzyme
- The enzyme's active site becomes more efficient.
- The enzyme molecules move too rapidly.
- The enzyme undergoes irreversible denaturation.
- The substrate molecules lose kinetic energy.
- Primary structure
- Peptide bonds
- Ionic bonds and hydrogen bonds in its active site
- Substrate concentration
- Are consumed during reactions
- Slow down metabolic processes
- Speed up biochemical reactions without being consumed
- Generate energy for cellular activities
- All enzymes have been denatured
- All active sites are occupied by substrate molecules
- The product concentration is zero
- The temperature is at its optimum
- Increased
- Decreased
- Unchanged
- Varied randomly
- Enzyme activity is constant across all pH values.
- Enzymes are active only at extreme pH levels.
- Deviations from optimal pH significantly reduce activity.
- Increasing pH always increases activity.
- Providing energy for the reaction
- Straining substrate bonds
- Forming new covalent bonds with the substrate
- Releasing the product immediately
