- Holoenzyme
- Coenzyme
- Apoenzyme
- Prosthetic group
Category: ENZYMES
- 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.
- The highest possible temperature
- A broad range of pH values
- Physiological conditions
- Very low substrate concentrations
- Competitive inhibitor
- Non-competitive inhibitor
- Substrate analogue
- Allosteric activator
- 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
- Coenzyme
- Substrate
- Apoenzyme
- Cofactor
- 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.
