Skip to main content

Enzyme-Substrate Complex quiz #2 Flashcards

Enzyme-Substrate Complex quiz #2
Control buttons has been changed to "navigation" mode.
1/30
  • What is the main reason enzymes are highly specific for their substrates?

    Because the active site is shaped to form optimal non-covalent interactions with specific substrates.
  • What is the fate of the substrate after binding to the enzyme?

    The substrate is converted into product while bound to the enzyme.
  • How does the formation of the enzyme-substrate complex affect the rate of product formation?

    It increases the rate of product formation by lowering the activation energy.
  • What is the main function of the enzyme in the enzyme-substrate complex?

    To catalyze the conversion of substrate to product by stabilizing the transition state.
  • What is the significance of the energy of activation in enzyme-catalyzed reactions?

    Lowering the energy of activation increases the reaction rate.
  • How does the enzyme-substrate complex contribute to the efficiency of enzymatic reactions?

    By facilitating substrate binding and transition state stabilization, making the reaction proceed faster.
  • What is the relationship between the enzyme-substrate complex and the active site?

    The enzyme-substrate complex forms when the substrate binds to the enzyme's active site.
  • Why are most interactions in the enzyme-substrate complex non-covalent?

    Non-covalent interactions allow for reversible binding and release of substrate and product.
  • What is the main advantage of the enzyme being released unaltered after the reaction?

    It allows the enzyme to catalyze multiple rounds of the reaction.
  • How does the enzyme-substrate complex relate to the concept of reaction intermediates?

    It is a specific example of a reaction intermediate in enzyme-catalyzed processes.
  • What is the effect of enzyme catalysis on the transition state energy?

    Enzyme catalysis lowers the transition state energy, making the reaction proceed faster.
  • What is the main role of binding energy in enzyme catalysis?

    Binding energy is used to stabilize the transition state and lower activation energy.
  • How does the enzyme-substrate complex contribute to the selectivity of enzyme reactions?

    Only substrates that fit well into the active site and form optimal interactions can form the complex.
  • What is the importance of the transient nature of the enzyme-substrate complex?

    It allows for rapid turnover and efficient catalysis.
  • How does the enzyme-substrate complex differ from the free enzyme and substrate?

    The complex is a bound intermediate, while the free enzyme and substrate are unbound.
  • What is the main function of the active site in the enzyme-substrate complex?

    To bind the substrate and facilitate its conversion to product.
  • How does the enzyme-substrate complex affect the thermodynamics of the reaction?

    It does not change the overall thermodynamics but lowers the activation energy.
  • What is the significance of the enzyme-substrate complex in biological systems?

    It enables efficient and specific catalysis of biochemical reactions.
  • How does the enzyme-substrate complex relate to the concept of catalysis?

    It is a key intermediate that allows the enzyme to catalyze the reaction.
  • What is the main reason for the high efficiency of enzymes?

    Their ability to stabilize the transition state through binding energy.
  • How does the enzyme-substrate complex facilitate the release of product?

    After catalysis, the product has lower affinity and is released, freeing the enzyme.
  • What is the main difference between covalent and non-covalent interactions in the enzyme-substrate complex?

    Non-covalent interactions are reversible and predominant, while covalent interactions are less common and usually transient.
  • How does the enzyme-substrate complex contribute to the regulation of metabolic pathways?

    By allowing specific and efficient catalysis, enzymes help regulate the flow of metabolites.
  • What is the main advantage of weak non-covalent forces in enzyme catalysis?

    They allow for rapid binding and release, enabling high turnover rates.
  • How does the enzyme-substrate complex ensure reaction specificity?

    Only substrates that fit the active site and form optimal interactions can be catalyzed.
  • What is the main outcome of the enzyme-substrate complex formation?

    Facilitation of the chemical reaction by lowering activation energy and increasing reaction rate.
  • How does the enzyme-substrate complex relate to the concept of induced fit?

    Binding of the substrate may induce conformational changes in the enzyme, optimizing catalysis.
  • What is the main role of the enzyme in the enzyme-substrate complex?

    To provide a catalytic environment that stabilizes the transition state and accelerates the reaction.
  • How does the enzyme-substrate complex affect the energy profile of a reaction?

    It introduces an intermediate energy minimum and lowers the transition state energy.
  • What is the significance of the enzyme being unaltered after the reaction?

    It allows the enzyme to participate in multiple catalytic cycles.