- Reversibility of binding.
- Effect on enzyme's Vmax?.
- Binding location on the enzyme.
- Chemical nature.
Category: ENZYMES
- Reusability
- Specificity
- Turnover rate
- Structural integrity
- Substrate concentration and product inhibition.
- Enzyme stability and collision frequency.
- pH changes and cofactor availability.
- Activation energy and free energy change.
- Irreversibly denature the enzyme.
- Bind to the allosteric site and activate the enzyme.
- Occupy the active site, preventing substrate binding.
- Convert directly into product.
- Product release
- Substrate binding
- Formation of the transition state
- Denaturation of the enzyme
- Direct binding of the substrate to the active site.
- Changes in pH or temperature.
- Binding of molecules at sites other than the active site.
- The formation of an irreversible enzyme-inhibitor complex.
- Secondary structure
- Quaternary structure
- Tertiary folding
- Denaturation
- Non-protein part of a conjugated enzyme.
- Protein part of a conjugated enzyme, lacking its cofactor.
- Complete, catalytically active enzyme.
- Substrate molecule that binds to the enzyme.
- Coenzyme
- Substrate
- Apoenzyme
- Cofactor
- All metabolic reactions are exothermic at this temperature.
- The enzymes are most stable at this temperature.
- It maximizes molecular collisions and catalytic efficiency without denaturation.
- This temperature is required for substrate binding.
- Increase the yield of products.
- Allow the equilibrium to be reached more quickly.
- Shift the equilibrium towards reactants.
- Prevent the reaction from reaching equilibrium.
- Substrate saturation
- Product inhibition
- Substrate inhibition
- Allosteric regulation
- Flexibility.
- Reusability.
- Unique active site shape for its substrate.
- Optimal pH.
- Irreversible inhibition of the enzyme.
- Changes in the enzyme's active site conformation and activity.
- Direct competition with the substrate.
- Formation of a permanent enzyme-inhibitor complex.
- Chemical nature (protein vs. non-protein).
- Necessity for enzyme activity.
- Type of binding to the apoenzyme (loosely vs. tightly/covalently).
- Role in catalysis.
- Increasing the kinetic energy of reactants.
- Forming new chemical bonds with the products.
- Orienting substrates and promoting the formation of the transition state.
- Consuming itself during the reaction.
- Primary structure.
- Covalent bonds.
- Non-covalent interactions that maintain its tertiary and quaternary structures.
- Substrate binding capacity only.
- Ligase
- Transferase
- Hydrolase
- Isomerase
