- Coenzyme
- Substrate
- Apoenzyme
- Cofactor
Category: Biology etea medical mcqs
- Primary amino acid sequence.
- Peptide bonds.
- Complex three-dimensional folding.
- Rate of synthesis.
- Reusability in a reaction.
- Specificity for a substrate.
- Maximum number of substrate molecules converted to product per unit time.
- Sensitivity to inhibitors.
- Increased activation energy.
- Competitive inhibition by the product.
- Non-competitive inhibition by the product.
- Both B and C are possible depending on the product.
- 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.
- 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.
