- Competing with the substrate for the active site.
- Denaturing the enzyme's protein structure by binding to SH groups.
- Increasing the activation energy of the reaction.
- Acting as cofactors for alternative pathways.
Category: Biology etea medical mcqs
- The enzyme's active site is rigid.
- Substrate binding causes a conformational change in the enzyme.
- Only perfect molecular fits are allowed.
- Enzymes act as simple locks.
- Ligase
- Isomerase
- Transferase
- Hydrolase
- Competitive inhibition
- Reversible inhibition
- Non-competitive inhibition
- Irreversible inhibition
- Apoenzyme
- Holoenzyme
- Substrate
- Prosthetic group
- Higher affinity for its substrate.
- Lower affinity for its substrate.
- Faster reaction rate.
- Slower reaction rate.
- Holoenzyme
- Coenzyme
- Apoenzyme
- Prosthetic group
- The maximum velocity of the reaction.
- The enzyme's sensitivity to temperature.
- The affinity of an enzyme for its substrate.
- The concentration of the enzyme.
- Prevents the overproduction of metabolic products.
- Increases the efficiency of enzyme synthesis.
- Ensures that all enzymes in a pathway are constantly active.
- Promotes the accumulation of intermediate products.
- Competitive inhibitor
- Non-competitive inhibitor
- Substrate analogue
- Allosteric activator
- The highest possible temperature
- A broad range of pH values
- Physiological conditions
- Very low substrate concentrations
- Highly reversible
- Specific to a single pathway
- Components of metabolic pathways
- Insensitive to temperature
- Primary amino acid sequence
- Covalent bonds within the active site
- Non-covalent interactions maintaining the 3D structure
- Substrate-enzyme complex formation
- 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.
- 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
- Concentration of product
- Availability of enzyme active sites
- Accumulation of inhibitors
- pH of the medium
- 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.
- Denatured
- Inhibited
- Saturated
- Activated
