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5: Michaelis-Menten Enzyme Kinetics, Inhibitors, pH optima; Bi-Substrate Reactions

  • Page ID
    165286
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    • 5.1: Catalytic Efficiency of Enzymes
      Enzymes are important for a variety of reasons, because they are involved in many vital biochemical reactions. Increasing the reaction rate of a chemical reaction allows the reaction to become more efficient, and hence more products are generated at a faster rate. These products then become involved in some other biological pathway that initiates certain functions of the human body. This is known as the catalytic efficiency of enzymes.
    • 5.2: 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.
    • 5.3: 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.
    • 5.4: Enzyme Inhibition
      An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. Not all molecules that bind to enzymes are inhibitors; enzyme activators bind to enzymes and increase their enzymatic activity, while enzyme substrates bind and are converted to products in the normal catalytic cycle of the enzyme.
    • 5.5: Temperature, pH, and enzyme concentration on the rate of a reaction
      This section will explore the effect of temperature, pH, and enzyme concentration on the rate of a reaction.
    • 5.6: Multi-Substrate Sequential Mechanisms
      Sequential reactions are one of the classes involved in multiple substrate reactions. In these types of reactions, all the substrates involved are bound to the enzyme before catalysis of the reaction takes place to release the products. Sequential reactions can be either ordered or random.
    • 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.


    5: Michaelis-Menten Enzyme Kinetics, Inhibitors, pH optima; Bi-Substrate Reactions is shared under a CC BY-NC-SA 4.0 license and was authored, remixed, and/or curated by LibreTexts.

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