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Chemistry LibreTexts

5: Michaelis-Menten Enzyme Kinetics

  • Page ID
    165194
    • 5.1: Catalytic Efficiency of Enzymes
    • 5.2: Michaelis-Menten Kinetics
      Two 20th century scientists, Leonor Michaelis and Maud Leonora Menten, proposed the model known as Michaelis-Menten Kinetics to account for enzymatic dynamics. The model serves to explain how an enzyme can cause kinetic rate enhancement of a reaction and explains how reaction rates depends on the concentration of enzyme and substrate.
    • 5.3: Enzyme Parameters
      Scientists spend a considerable amount of time characterizing enzymes. To understand how they do this and what the characterizations tell us, we must first understand a few parameters. Imagine I wished to study the reaction catalyzed by an enzyme I have just isolated. I would be interested to understand how fast the enzyme works and how much affinity the enzyme has for its substrate(s).
    • 5.4: Enzyme Inhibition
    • 5.5: Temperature, pH, and enzyme concentration on the rate of a reaction
    • 5.6: Multi-Substrate Sequential Mechanisms
    • 5.7: Double displacement reaction
      Ping-pong mechanism, also called a double-displacement reaction, is characterized by the change of the enzyme into an intermediate form when the first substrate to product reaction occurs. It is important to note the term intermediate indicating that this form is only temporary. A key characteristic of the ping-pong mechanism is that one product is formed and released before the second substrate binds.

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