- The formation of final products.
- Maximum stability of the enzyme-substrate complex.
- An unstable, high-energy intermediate where bonds are being broken/formed.
- The enzyme's release from the product.
No category found.
- Ligase
- Isomerase
- Hydrolase
- Transferase
- Accelerate a wider range of reactions.
- Maintain cellular homeostasis with minimal resources.
- Increase the overall yield of product.
- Denature easily at high temperatures.
- Substrates
- Coenzymes
- Products
- Active sites
- Permanently alters the enzyme's active site.
- Reduces the free energy of the products.
- Orients substrates correctly and strains their bonds for reaction.
- Increases the temperature of the reaction.
- Substrate concentration required for half maximal velocity.
- Maximum rate at which an enzyme can catalyze a reaction.
- Energy required to initiate the reaction.
- Concentration of product at equilibrium.
- Their active site changes its charge distribution, repelling the substrate.
- The enzyme's primary structure is broken down by strong acids/bases.
- Ionic and hydrogen bonds maintaining the enzyme's 3D structure are disrupted.
- Substrate molecules become denatured at extreme pH.
- Competes for the active site.
- Binds to an allosteric site, altering enzyme efficiency.
- Forms a permanent bond with the enzyme.
- Increases the enzyme's affinity for its substrate.
- Cofactor.
- Product.
- Substrate.
- Allosteric modulator.
- The enzyme is denatured.
- All active sites are continuously occupied.
- Product accumulation becomes inhibitory.
- The optimal temperature has been exceeded.
- Anabolic catalysts.
- Catabolic catalysts.
- Irreversible inhibitors.
- Allosteric regulators.
- The presence of inorganic cofactors only.
- The sequence of nucleotides.
- The precise three-dimensional folding of amino acid chains.
- Their ability to form peptide bonds with substrates.
- Reduce the enzyme's Vmax?.
- Have a similar structure to the substrate.
- Bind to an allosteric site.
- Cannot be displaced by increasing substrate.
- Free energy change.
- Binding energy.
- Activation energy.
- Kinetic energy.
- Reusability.
- Specificity.
- Dynamic and flexible structure.
- High turnover rate.
- Increasing substrate concentration.
- Irreversible changes in enzyme structure.
- Reversible inhibition.
- Increased product formation.
- It allows for constant enzyme synthesis.
- A small amount of enzyme can process a large amount of substrate quickly.
- It makes the enzyme more resistant to denaturation.
- It reduces the overall free energy change of the reaction.
- The initial binding of substrate to enzyme.
- The final release of product from enzyme.
- An unstable intermediate where substrate is partially converted.
- The denaturation of the enzyme.
- The enzyme is working at suboptimal conditions.
- The substrate concentration is limiting.
- The enzyme's active sites are saturated with substrate.
- Product inhibition is occurring.
