- Increase the activation energy of the reaction.
- Prevent the formation of transition state.
- Lower the activation energy of the reaction.
- Shift the reaction equilibrium towards reactants.
No category found.
- Increased enzyme stability
- Enhanced product formation
- Reduced or absent substrate binding
- A shift in optimal temperature
- Primary and secondary structures
- Secondary and tertiary structures
- Primary and quaternary structures
- Tertiary and quaternary structures
- Changes in substrate concentration.
- Alteration of the active site's charge and shape.
- Irreversible breaking of peptide bonds.
- Formation of too many enzyme-product complexes.
- Concentration of product
- Availability of enzyme active sites
- Accumulation of inhibitors
- pH of the medium
- Denatured
- Inhibited
- Saturated
- Activated
- Coenzyme
- Substrate
- Apoenzyme
- Cofactor
- Reusability in a reaction.
- Specificity for a substrate.
- Maximum number of substrate molecules converted to product per unit time.
- Sensitivity to inhibitors.
- Primary amino acid sequence.
- Peptide bonds.
- Complex three-dimensional folding.
- Rate of synthesis.
- 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.
- Positive feedback
- Competitive inhibition
- Feedback inhibition
- Irreversible inhibition
- 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.
- 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.
- 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.
- 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
- Lock and key hypothesis
- Induced fit model
- Allosteric regulation
- Competitive inhibition
- Remain unchanged
- Double
- Halve
- Increase by a factor of four
