- Catalyze any biochemical reaction in the cell.
- Bind to a broad range of molecules for catalysis.
- Exert their catalytic effect on particular substrates.
- Function optimally across a wide range of pH values.
Category: Biology etea medical mcqs
- Increased affinity of the enzyme for its substrate.
- A change in the shape of the active site, reducing its catalytic efficiency.
- Direct competition with the substrate for the active site.
- Formation of a new enzyme-substrate complex.
- Positive feedback
- Competitive inhibition
- Feedback inhibition
- Irreversible inhibition
- Shifting the equilibrium towards product formation.
- Increasing the kinetic energy of reactant molecules.
- Providing an alternative reaction pathway with a lower activation energy.
- Decreasing the overall free energy change of the reaction.
- The active site remains rigid and functional.
- Molecular motion is slowed down, not structural integrity lost.
- Substrate molecules denature before the enzyme.
- The enzyme becomes more specific at low temperatures.
- Ability to alter the enzyme's allosteric site.
- Structural similarity to the actual substrate.
- High molecular weight.
- Irreversible binding to the enzyme.
- Increased enzyme-substrate affinity
- More effective lowering of activation energy
- Disruption of the enzyme's specific 3D structure
- Faster product formation
- Remain unchanged
- Double
- Halve
- Increase by a factor of four
- Lock and key hypothesis
- Induced fit model
- Allosteric regulation
- Competitive inhibition
- Ligase
- Isomerase
- Hydrolase
- Transferase
- The formation of final products.
- Maximum stability of the enzyme-substrate complex.
- An unstable, high-energy intermediate where bonds are being broken/formed.
- The enzyme's release from the product.
- Substrates
- Coenzymes
- Products
- Active sites
- Accelerate a wider range of reactions.
- Maintain cellular homeostasis with minimal resources.
- Increase the overall yield of product.
- Denature easily at high temperatures.
- Permanently alters the enzyme's active site.
- Reduces the free energy of the products.
- Orients substrates correctly and strains their bonds for reaction.
- Increases the temperature of the reaction.
- Their active site changes its charge distribution, repelling the substrate.
- The enzyme's primary structure is broken down by strong acids/bases.
- Ionic and hydrogen bonds maintaining the enzyme's 3D structure are disrupted.
- Substrate molecules become denatured at extreme pH.
- 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.
- 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.
