Enzyme

• What is the definition of an enzyme?

  Enzymes are proteins that function as biological catalysts.
• Why are enzymes important in the body?

  They catalyze all chemical reactions necessary for life.
• What happens if enzymes do not work correctly?

  It can lead to metabolic disorders, such as Alkaptonuria.
• What is one use of enzymes in medicine?

  They can be used as therapeutic agents, like statins.
• What is the role of co-factors and co-enzymes in enzyme function?

  They assist enzymes in catalyzing reactions.
• What is the effect of temperature on enzyme activity?

  Enzymes operate best between 35-40°C.
• What is the significance of the Michaelis-Menton constant (Km)?

  It reflects the affinity of an enzyme for its substrate.
• How do isoenzymes differ from regular enzymes?

  Isoenzymes differ in amino acid sequences but catalyze the same reaction.
• What is the role of an active site in an enzyme?

  The active site is where substrate binding occurs.
• What is the formula for the Michaelis-Menton equation?

  V = $\frac{V_{max} [S]}{K_m + [S]}$
• What is the difference between competitive and non-competitive inhibitors?

  Competitive inhibitors bind to the active site, while non-competitive inhibitors bind elsewhere.
• What are the factors that regulate enzyme activity?

  1. Temperature
  2. pH
  3. Substrate concentration
  4. Cofactors/Coenzymes
  5. Enzyme Inhibition
• What are the key features of the Lineweaver-Burk plot?

  • It is a double reciprocal plot.
  • Illustrates kinetic data linearly.
  • Allows accurate calculation of $V_{max}$ and $K_m$.
• What are the types of enzyme inhibitors?

  • Irreversible Inhibitors: Form covalent bonds, cannot regain activity.
  • Reversible Inhibitors: Bind non-covalently, activity can be restored.
• What is the significance of enzyme kinetics in studying enzymes?

  • Helps understand reaction rates.
  • Provides insights into enzyme efficiency.
  • Aids in drug development targeting enzymes.
• What is the difference between apoenzyme and holoenzyme?

  • Apoenzyme: Enzyme without cofactor (inactive).
  • Holoenzyme: Enzyme with cofactor (active).
• What is the effect of pH on enzyme activity?

  • Each enzyme has an optimum pH.
  • Extreme pH can cause denaturation.
  • Affects amino acid side-chains in the active site.
• What is the relationship between substrate concentration and enzyme activity?

  • Rate increases with substrate concentration until $V_{max}$ is reached.
  • Important for metabolic control.
  • Different enzymes have different $K_m$ values.
• What is the role of coenzymes in enzyme function?

  • Organic molecules that assist enzymes.
  • Often derived from vitamins.
  • May be transiently associated with the enzyme.
• What is the significance of enzyme specificity?

  • Each enzyme binds to specific substrates.
  • Catalyzes specific reactions.
  • Ensures metabolic pathways function correctly.
• What is the importance of studying enzymes in diagnostics?

  • Enzymes can indicate disease presence.
  • Used in clinical tests for various conditions.
  • Help monitor health and treatment efficacy.