- Substrate concentration required for half maximal velocity.
- Maximum rate at which an enzyme can catalyze a reaction.
- Energy required to initiate the reaction.
- Concentration of product at equilibrium.
Category: Biology etea medical mcqs
- Competes for the active site.
- Binds to an allosteric site, altering enzyme efficiency.
- Forms a permanent bond with the enzyme.
- Increases the enzyme's affinity for its substrate.
- Cofactor.
- Product.
- Substrate.
- Allosteric modulator.
- The enzyme is denatured.
- All active sites are continuously occupied.
- Product accumulation becomes inhibitory.
- The optimal temperature has been exceeded.
- Anabolic catalysts.
- Catabolic catalysts.
- Irreversible inhibitors.
- Allosteric regulators.
- The presence of inorganic cofactors only.
- The sequence of nucleotides.
- The precise three-dimensional folding of amino acid chains.
- Their ability to form peptide bonds with substrates.
- Reduce the enzyme's Vmax?.
- Have a similar structure to the substrate.
- Bind to an allosteric site.
- Cannot be displaced by increasing substrate.
- Reusability.
- Specificity.
- Dynamic and flexible structure.
- High turnover rate.
- Free energy change.
- Binding energy.
- Activation energy.
- Kinetic energy.
- Increasing substrate concentration.
- Irreversible changes in enzyme structure.
- Reversible inhibition.
- Increased product formation.
- It allows for constant enzyme synthesis.
- A small amount of enzyme can process a large amount of substrate quickly.
- It makes the enzyme more resistant to denaturation.
- It reduces the overall free energy change of the reaction.
- The enzyme is working at suboptimal conditions.
- The substrate concentration is limiting.
- The enzyme's active sites are saturated with substrate.
- Product inhibition is occurring.
- The initial binding of substrate to enzyme.
- The final release of product from enzyme.
- An unstable intermediate where substrate is partially converted.
- The denaturation of the enzyme.
- Substrate denaturation.
- Protonation or deprotonation of amino acid residues in the active site.
- Increased kinetic energy of the enzyme.
- Formation of excessive enzyme-product complexes.
- All reactions occur simultaneously.
- Only specific reactions are catalyzed at appropriate times.
- Enzymes are reused continuously.
- The cell maintains a constant temperature.
- Increasing the random collisions between molecules.
- Providing an alternative reaction pathway.
- Directly altering the concentration of reactants.
- Supplying heat to the reaction.
- Increase the free energy of the system.
- Speed up the attainment of equilibrium.
- Make an endergonic reaction exergonic.
- Generate energy for cellular processes.
- An inorganic molecule.
- A metal ion.
- An organic molecule, often a vitamin derivative.
- Tightly bound to the enzyme.
- Increased substrate affinity.
- Enhanced molecular motion.
- Denaturation of the enzyme's active site.
- Decrease in substrate concentration.
