Enzyme Function and Regulation

Revision sheet excerpt

Course Outline

  1. Enzyme Modes of Action
  2. Factors Influencing Enzyme Activity
  3. Metabolic Pathways in Cells
  4. Biochemistry of Cells
  5. Enzyme Properties and Nomenclature
  6. Enzyme Classification Types
  7. Enzyme Catalysis Mechanism
  8. Effects of pH and Temperature
  9. Enzyme Inhibition Types
  10. Enzyme Cofactors and Coenzymes

1. Enzyme Modes of Action

Key Concepts & Definitions

  • Enzyme modes of action: The specific ways enzymes facilitate biochemical reactions by lowering activation energy, primarily through the formation of an enzyme-substrate complex. (implied from context)

  • Enzyme-substrate complex: An intermediate formed when the substrate binds to the enzyme's active site, enabling the reaction to proceed more efficiently. (implied from context)

  • Lock-and-key model: A hypothesis describing enzyme action where the enzyme's active site and the substrate have complementary shapes, fitting together perfectly without change in enzyme structure. (hypothesized as a model of enzyme-substrate interaction)

  • Induced fit model: A hypothesis proposing that the binding of substrate induces a conformational change in the enzyme, resulting in a better fit between enzyme and substrate, thus facilitating the reaction. (hypothesized as a model of enzyme-substrate interaction)

Essential Points

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Quiz preview

1. Who is credited with proposing the induced fit model of enzyme action?

2. When was the lock-and-key model of enzyme action first proposed?

3. What is an enzyme primarily considered to be in biochemical reactions?

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Flashcards preview

Enzyme modes of action

Lower activation energy via substrate binding.

Enzyme-substrate complex

Intermediate formed during catalysis.

Lock-and-key model

Active site and substrate are complementary.

Induced fit model

Enzyme changes shape upon substrate binding.

Factors influencing activity

Substrate, temperature, pH, inhibitors.

Substrate saturation

All active sites occupied; max rate.

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