- Catalyze irreversible reactions.
- Bind to a wider range of substrates.
- Adapt their shape slightly to better fit the substrate.
- Function without a specific active site.
No category found.
- The enzyme is being denatured by excess substrate.
- The reaction reaches equilibrium.
- All enzyme active sites become occupied.
- Product accumulation inhibits the reaction.
- How many times it can be reused.
- The rate at which it denatures.
- How many substrate molecules it can convert per unit time.
- Its sensitivity to pH.
- Availability of cofactors.
- Concentration of enzyme molecules.
- Number of active sites available for substrate binding.
- Optimal pH of the reaction.
- Reversible competitive inhibitor
- Irreversible inhibitor
- Allosteric activator
- Non-competitive allosteric activator
- Reusability
- Specificity
- Temperature optimum
- pH optimum
- Isomerase
- Hydrolase
- Ligase
- Lyase
- Cause denaturation.
- Slow down molecular motion.
- Irreversibly alter the active site.
- Increase activation energy.
- Ability to bind to an allosteric site.
- Tendency to form temporary bonds with the enzyme.
- Structural similarity to the substrate.
- Effect on the enzyme's Vmax?.
- Cofactor molecule
- Inhibitor molecule
- Substrate molecule
- Product molecule
- Becomes rigid upon substrate binding.
- Changes shape slightly to better accommodate the substrate.
- Can bind to any molecule.
- Is identical for all enzymes.
- Increasing overall product yield.
- Maintaining cellular energy balance.
- Preventing wasteful overproduction of substances.
- Accelerating the metabolic pathway.
- Reversibility of binding.
- Effect on enzyme's Vmax?.
- Binding location on the enzyme.
- Chemical nature.
- 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
