- Flexibility.
- Reusability.
- Unique active site shape for its substrate.
- Optimal pH.
Category: Biology etea medical mcqs
- Irreversible inhibition of the enzyme.
- Changes in the enzyme's active site conformation and activity.
- Direct competition with the substrate.
- Formation of a permanent enzyme-inhibitor complex.
- Chemical nature (protein vs. non-protein).
- Necessity for enzyme activity.
- Type of binding to the apoenzyme (loosely vs. tightly/covalently).
- Role in catalysis.
- Increasing the kinetic energy of reactants.
- Forming new chemical bonds with the products.
- Orienting substrates and promoting the formation of the transition state.
- Consuming itself during the reaction.
- Primary structure.
- Covalent bonds.
- Non-covalent interactions that maintain its tertiary and quaternary structures.
- Substrate binding capacity only.
- Ligase
- Transferase
- Hydrolase
- Isomerase
- Permanently altering the enzyme's active site.
- Binding to the enzyme at a site other than the active site.
- Competing with the substrate for binding to the active site.
- Increasing the activation energy of the reaction.
- Limited substrate availability.
- High product concentration.
- Saturating substrate concentration.
- Optimal temperature has not been reached.
- Reversible competitive inhibition.
- Irreversible non-competitive inhibition.
- Allosteric activation.
- Increased substrate affinity.
- Around 37?C
- Below 20?C
- Above 70?C
- In the acidic range
- Their solubility in water.
- Their heat resistance.
- The formation of specific active sites.
- Their ability to transport substances across membranes.
- Provides alternative reaction pathways with higher activation energies.
- Increases the energy of the reactants.
- Stabilizes the transition state, lowering the activation energy.
- Shifts the equilibrium to favor product formation.
- Increase the reaction rate proportionally.
- Further increase the reaction rate, but less steeply.
- Have no significant effect on the reaction rate.
- Decrease the reaction rate due to substrate inhibition.
- Increased kinetic energy of molecules.
- Alteration of ionic bonds and hydrogen bonds, changing active site shape.
- Increased substrate affinity.
- Formation of excessive enzyme-product complexes.
- Allosteric regulation
- Induced fit model
- Feedback inhibition
- Transition state theory
- Amino acid sequence of its active site.
- Overall molecular weight of the enzyme.
- Presence of cofactors.
- Temperature of the reaction.
- All enzymes would stop functioning.
- Specific enzyme-catalyzed reactions would be impaired.
- Substrate molecules would become denatured.
- Product synthesis would increase uncontrollably.
- Coenzyme
- Substrate analogue
- Feedback activator
- Feedback inhibitor
- Random interaction between enzyme and substrate.
- The enzyme's denaturation.
- Proper orientation and proximity of reactants for chemical change.
- Irreversible binding of the substrate.
