Enzyme Substrate Interaction and Michaelis-Menten Equation
30 Questions
1 Views

Choose a study mode

Play Quiz
Study Flashcards
Spaced Repetition
Chat to lesson

Podcast

Play an AI-generated podcast conversation about this lesson

Questions and Answers

What happens to the rate of an enzyme-catalyzed reaction when the substrate concentration becomes the limiting factor?

  • It remains constant with any further increase in enzyme concentration
  • It becomes independent of the enzyme concentration (correct)
  • It decreases with any further increase in enzyme concentration
  • It continues to increase with any further increase in enzyme concentration
  • What is the relationship between enzyme concentration and reaction rate when substrate concentration is not limiting?

  • Directly proportional (correct)
  • Exponential
  • Inverse
  • Independent
  • What is the significance of the Q10 value in enzyme-controlled reactions?

  • Predicts the enzyme's pH optimum
  • Determines the enzyme specificity
  • Quantifies the rate increase with temperature rise (correct)
  • Indicates the enzyme's optimal temperature
  • Why do cold-water fish die at 30°C?

    <p>Their enzymes denature at this temperature</p> Signup and view all the answers

    What happens to most enzymes at 70°C?

    <p>They denature completely</p> Signup and view all the answers

    What is the pH range preferred by most enzymes for optimal activity?

    <p>Neutral (pH 6-8)</p> Signup and view all the answers

    What induces a change in the enzyme's conformation when it combines with a substrate?

    <p>Stretching of substrate bonds</p> Signup and view all the answers

    What is the primary function of the active site of an enzyme?

    <p>To make the chemical environment suitable for the reaction</p> Signup and view all the answers

    In the Michaelis-Menten equation, what does the KS constant stand for?

    <p>Enzyme-substrate complex concentration</p> Signup and view all the answers

    According to Michaelis and Menten's assumptions, what is a key aspect of the enzymatic reaction?

    <p>Low substrate concentration compared to enzymes</p> Signup and view all the answers

    What is the primary focus of the Michaelis-Menten equation?

    <p>Velocity of enzymatic reactions with a single substrate</p> Signup and view all the answers

    What is one assumption made by Michaelis and Menten about enzyme reactions?

    <p>The process continues essentially to its completion</p> Signup and view all the answers

    What is the Michaelis-Menten constant denoted by in the given equation?

    <p>Km</p> Signup and view all the answers

    How is enzyme activity commonly expressed?

    <p>Moles of substrate converted to product per unit time</p> Signup and view all the answers

    Why does the rate of an enzyme-catalyzed reaction increase with an increase in substrate concentration?

    <p>More substrate molecules collide with enzyme molecules</p> Signup and view all the answers

    In what scenario would the initial rate of an enzyme-catalyzed reaction be proportional to the concentration of enzyme ([E])?

    <p>[S] &gt; [E]</p> Signup and view all the answers

    How does an increase in enzyme concentration affect the reaction rate?

    <p>Increases reaction rate</p> Signup and view all the answers

    At what point does an enzyme become saturated in terms of substrate concentration?

    <p>When further increase in substrate has no effect on reaction rate</p> Signup and view all the answers

    What is the primary role of inorganic metal ions in enzyme catalysis?

    <p>Forming coordination bonds with side chains at the active site</p> Signup and view all the answers

    Which coenzyme is responsible for transferring acyl groups during metabolic reactions?

    <p>Coenzyme A</p> Signup and view all the answers

    What is the function of a transient carrier coenzyme in biochemical reactions?

    <p>Transferring specific atoms or functional groups</p> Signup and view all the answers

    Which vitamin serves as a dietary precursor for mammals and is essential for various carboxylation reactions?

    <p>Biotin</p> Signup and view all the answers

    What is the main function of inhibitors on enzyme activities?

    <p>To lower the enzyme's catalytic rate</p> Signup and view all the answers

    Which inorganic element acts as a cofactor for the enzyme carbonic anhydrase?

    <p>Zn2+</p> Signup and view all the answers

    What is a coenzyme when it comes to enzyme cofactors?

    <p>An organic compound</p> Signup and view all the answers

    Which type of cofactor is referred to as a prosthetic group?

    <p>Organic or inorganic compounds tightly bound to the apoenzyme</p> Signup and view all the answers

    What is the composition of a holoenzyme?

    <p>Apoenzyme + Coenzyme</p> Signup and view all the answers

    In enzyme catalysis, coenzymes often function as what?

    <p>Intermediate carriers of electrons</p> Signup and view all the answers

    What role does NAD play in certain oxidations/reductions?

    <p>Carrier of electrons</p> Signup and view all the answers

    What distinguishes coenzymes from other enzyme cofactors?

    <p>Their association with the enzyme is transient</p> Signup and view all the answers

    Study Notes

    Enzyme Catalysed Reactions

    • The rate of an enzyme-catalysed reaction is directly proportional to the enzyme concentration when the substrate concentration is not limiting.
    • Increasing enzyme concentration will increase the rate of reaction until the substrate concentration becomes the limiting factor.

    Effect of Temperature on Velocity

    • Enzymes have an optimal temperature, with a balance between the Q10 (temperature coefficient) and denaturation.
    • Q10 is the increase in reaction rate with a 10°C rise in temperature, with a typical value of 2-3 for chemical reactions.
    • Most enzymes are fully denatured at 70°C, but some can withstand high temperatures up to 100°C.

    Effect of pH Value on Velocity

    • The pH optimum varies for different enzymes, with most having a neutral pH (6-8).
    • When a substrate combines with an enzyme, it induces a change in the enzyme's conformation, making the chemical environment suitable for the reaction.

    Michaelis-Menten Equation

    • The Michaelis-Menten equation describes the velocity of enzymatic reactions, with the equation: VO = Vmax[S] / Km + [S]
    • VO is the initial velocity of the reaction, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration.

    Enzyme Velocity and Activity

    • Enzyme activity is expressed by the initial rate (V0) of the reaction being catalyzed.
    • Enzyme activity is measured in moles of substrate converted to product per unit time.
    • Velocity decreases as time increases due to factors such as substrate depletion, product inhibition, pH change, and cofactor depletion.

    Effect of Substrate Concentration

    • An increase in substrate concentration increases the rate of enzyme-catalysed reaction, but eventually reaches a point of saturation where further increases have no effect.

    Effect of Enzyme Concentration

    • The initial rate of an enzyme-catalysed reaction is proportionate to the concentration of enzyme.

    Coenzymes and Cofactors

    • Coenzymes are organic molecules that are derivatives of vitamins and act as transient carriers of specific atoms or functional groups.
    • Examples of coenzymes include Coenzyme A, Flavin adenine dinucleotide, and Nicotinamide adenine dinucleotide.
    • Inorganic metal ions such as Cu2+, Fe2+/Fe3+, K+, Mg2+, Mn2+, Mo, Ni2+, Se, and Zn2+ serve as cofactors by forming coordination bonds with side chains at the active site and with the substrate.

    Inhibition of Enzyme Activities

    • Inhibitors are molecules that act directly on an enzyme to lower its catalytic rate, often at low concentrations and with specificity.
    • Cofactors can be organic compounds (coenzymes) or inorganic groups (metal ions).
    • Prosthetic groups are organic or inorganic compounds that are tightly bound to the apoenzyme.

    Studying That Suits You

    Use AI to generate personalized quizzes and flashcards to suit your learning preferences.

    Quiz Team

    Description

    Learn about how substrates combine with enzymes to induce a change in conformation, create a suitable chemical environment for reactions, and lower the activation energy. Explore the Michaelis-Menten equation and different mechanisms of enzyme reactions proposed by biochemists.

    More Like This

    Use Quizgecko on...
    Browser
    Browser