- Inhibit the enzyme's action
- Alter the pH of the reaction
- Enhance catalytic activity by assisting in substrate binding or catalysis
- Denature the enzyme
Category: Biology etea medical mcqs
- 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
- Specificity
- Turnover rate
- Reusability
- Catalytic power
- Saturation point
- Denaturation point
- Transition state
- Optimum condition
- Allosteric activator
- Reversible competitive inhibitor
- Irreversible inhibitor
- Non-competitive inhibitor
- Primary structure
- Secondary structure
- Tertiary and Quaternary structures
- Peptide bonds
- An increase in enzyme activity
- A decrease in enzyme activity
- No change in enzyme activity
- Irreversible enzyme denaturation
- Allosteric regulation
- High turnover rate
- Specificity
- Reusability
- Substrate concentration is limiting
- Product concentration is high
- Substrate concentration is saturating
- Temperature is below optimum
- Lowering the temperature
- Increasing the pH
- Decreasing the substrate concentration
- Increasing the substrate concentration
- Primary structure
- Peptide bonds
- Hydrogen bonds and disulfide bridges
- Amino acid sequence
- Is perfectly rigid and unchanging
- Changes its conformation slightly upon substrate binding
- Can bind to multiple types of substrates simultaneously
- Is permanently altered after product release
- Providing additional energy to reactants
- Lowering the activation energy requirement
- Shifting the equilibrium towards products
- Increasing the collision frequency of reactants
