2.4.1 Enzyme action

• What is the primary role of enzymes in chemical reactions?

  Biological catalysts
• Enzymes operate within a narrow temperature and pH range.


  True
• Enzymes have a high level of specificity
• What change occurs in the active site when the substrate binds?

  Induced fit
• What is the overall structure of an enzyme besides the active site?

  Larger 3D structure
• How does the induced fit model differ from the lock-and-key model?

  Active site changes shape
• Enzymes are essential for high reaction rates in biological processes.


  True
• The lock-and-key model emphasizes the importance of a complementary fit between the active site and substrate.
• What does the lock-and-key model describe?

  Enzyme-substrate interaction
• The lock-and-key model explains how enzymes achieve high specificity in catalyzing reactions.


  True
• The induced fit model improves the enzyme's catalytic efficiency and specificity
• What is formed when the substrate binds to the active site of the enzyme?

  Enzyme-substrate complex
• The induced fit allows the active site to mold around the substrate, enhancing enzyme specificity.


  True
• What does the enzyme lower within the active site to speed up the reaction rate?

  Activation energy
• The complementary shape and induced fit of the active site are crucial for enzyme catalytic efficiency.

  True
• The complementary shape and induced fit of the active site allow the enzyme to properly position the substrate
• What are enzymes primarily defined as in biological reactions?

  Biological catalysts
• The active site of an enzyme undergoes induced fit to optimize substrate binding.


  True
• The lock-and-key model emphasizes the high specificity of enzymes due to the exact complementary shapes of the active site and the substrate
• The lock-and-key model proposes an exact
• What enhances both catalytic efficiency and specificity in the induced fit model?

  Conformational change
• Steps involved in enzyme catalysis:

  1️⃣ Enzyme-Substrate Complex Formation

  2️⃣ Activation Energy Reduction

  3️⃣ Product Release
• What is crucial for catalytic efficiency in enzymes?

  Complementary shape
• At what pH does pepsin in the stomach function optimally?

  pH 2
• What does Vmax represent in enzyme kinetics?

  Maximum reaction rate
• Enzymes speed up chemical reactions without being consumed
• What are the three key differences between enzymes and non-enzyme catalysts?

  Speed, specificity, consumption
• The active site of an enzyme has a complementary shape to the substrate.


  True
• The active site is the specific region on the enzyme where the substrate binds.
• The lock-and-key model describes the enzyme's active site as perfectly rigid.

  True
• The induced fit model enhances enzyme specificity and catalytic efficiency.
• What is the conformational change that optimizes substrate binding called?

  Induced fit
• The induced fit model involves a change in the active site's shape upon substrate binding.


  True
• The lock-and-key model proposes that the enzyme's active site has a shape that perfectly complements the substrate
• What change occurs in the induced fit model when the substrate binds to the active site?

  Conformational change
• The induced fit model enhances the enzyme's ability to bind the substrate more effectively.


  True
• The induced fit creates a tighter and more complementary binding between the enzyme and the substrate
• Steps involved in enzyme catalysis

  1️⃣ Enzyme-Substrate Complex Formation

  2️⃣ Catalytic Mechanism

  3️⃣ Product Release
• After product release, the enzyme is regenerated and ready to catalyze the next reaction
• What is the role of the active site's shape in enzyme function?

  Complementary binding