- Enzyme molecules start to denature.
- Product inhibition becomes dominant.
- There are fewer enzyme-substrate collisions.
- The activation energy increases.
No category found.
- To ensure it can bind to any molecule.
- To allow for non-specific catalysis.
- To facilitate specific substrate binding and effective catalysis.
- To prevent denaturation at high temperatures.
- Specificity
- Sensitivity
- Reusability
- Saturation
- React with all available substrates.
- Form a stable complex with the product.
- Provide a microenvironment conducive to bond rearrangement.
- Increase the kinetic energy of reactants.
- Allosteric site
- Regulatory site
- Binding site
- Active site
- Denaturation
- No activity
- Reduced activity
- Optimal activity
- 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.
- 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.
- Ligase
- Isomerase
- Transferase
- Hydrolase
- Competitive inhibition
- Reversible inhibition
- Non-competitive inhibition
- Irreversible inhibition
- Apoenzyme
- Holoenzyme
- Substrate
- Prosthetic group
- Holoenzyme
- Coenzyme
- Apoenzyme
- Prosthetic group
- Higher affinity for its substrate.
- Lower affinity for its substrate.
- Faster reaction rate.
- Slower reaction rate.
- 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
- Primary amino acid sequence
- Covalent bonds within the active site
- Non-covalent interactions maintaining the 3D structure
- Substrate-enzyme complex formation
- Highly reversible
- Specific to a single pathway
- Components of metabolic pathways
- Insensitive to temperature
