- Allosteric regulation
- High turnover rate
- Specificity
- Reusability
No category found.
- Substrate concentration is limiting
- Product concentration is high
- Substrate concentration is saturating
- Temperature is below optimum
- Lowering the temperature
- Increasing the pH
- Decreasing the substrate concentration
- Increasing the substrate concentration
- 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
- Primary structure
- Peptide bonds
- Hydrogen bonds and disulfide bridges
- Amino acid sequence
- 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
- 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
- Sensitivity to substrate concentration
- Specificity to temperature
- Adaptability to environmental conditions
- Ir Requirement for cofactors
- 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
- Product complex
- Substrate complex
- Transition state
- Active site
- Ability to lower activation energy
- Three-dimensional structure
- Sensitivity to temperature changes
- High molecular weight
- Enzymes become part of the final product.
- Enzymes are consumed in the reaction.
- Enzymes remain unchanged chemically.
- Enzymes increase the activation energy.
- Monosaccharides
- Fatty acids
- Amino acids
- Nucleotides
- Decreases linearly
- Remains constant
- Increases until an optimum, then decreases
- Increases indefinitely
- Reusability
- Specificity
- Catalytic efficiency
- Sensitivity to pH
- Compete with the substrate at the active site.
- Form strong, often covalent, bonds with the enzyme.
- Are easily removed by increasing substrate concentration.
- Only reduce enzyme activity temporarily.
- Competitive inhibition
- Allosteric regulation impairment
- Irreversible active site modification
- Substrate deficiency
