- Enzyme activity is constant across all pH values.
- Enzymes are active only at extreme pH levels.
- Deviations from optimal pH significantly reduce activity.
- Increasing pH always increases activity.
Category: ENZYMES
- Providing energy for the reaction
- Straining substrate bonds
- Forming new covalent bonds with the substrate
- Releasing the product immediately
- Specificity
- Turnover rate
- Reusability
- Catalytic power
- Saturation point
- Denaturation point
- Transition state
- Optimum condition
- Allosteric activator
- Reversible competitive inhibitor
- Irreversible inhibitor
- Non-competitive inhibitor
- Primary structure
- Secondary structure
- Tertiary and Quaternary structures
- Peptide bonds
- An increase in enzyme activity
- A decrease in enzyme activity
- No change in enzyme activity
- Irreversible enzyme denaturation
- Substrate concentration is limiting
- Product concentration is high
- Substrate concentration is saturating
- Temperature is below optimum
- Allosteric regulation
- High turnover rate
- Specificity
- Reusability
- Lowering the temperature
- Increasing the pH
- Decreasing the substrate concentration
- Increasing the substrate concentration
- Primary structure
- Peptide bonds
- Hydrogen bonds and disulfide bridges
- Amino acid sequence
- Is perfectly rigid and unchanging
- Changes its conformation slightly upon substrate binding
- Can bind to multiple types of substrates simultaneously
- Is permanently altered after product release
- Providing additional energy to reactants
- Lowering the activation energy requirement
- Shifting the equilibrium towards products
- Increasing the collision frequency of reactants
- A decrease in reaction rate
- No change in reaction rate
- A proportional increase in reaction rate
- An initial increase followed by a plateau
- Sensitivity to substrate concentration
- Specificity to temperature
- Adaptability to environmental conditions
- Ir Requirement for cofactors
- Binding to the active site directly
- Increasing the enzyme's optimal temperature
- Altering the shape of the active site indirectly
- Competing with the substrate for binding
- The enzyme has been denatured.
- The activation energy has become too high.
- All active sites are saturated with substrate.
- Product inhibition has occurred.
- Allosteric regulation model
- Induced fit model
- Lock and key model
- Feedback inhibition mechanism
- Ability to lower activation energy
- Three-dimensional structure
- Sensitivity to temperature changes
- High molecular weight
