Biochemistry Quiz: Enzymes and Coenzymes
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Questions and Answers

Which of the following statements is true regarding the Michaelis constant?

  • A low value of the Michaelis constant indicates low affinity for a substrate. (correct)
  • Competitive inhibitors can decrease the value of the Michaelis constant.
  • Noncompetitive inhibitors can increase the value of the Michaelis constant.
  • A high value of the Michaelis constant indicates high affinity for a substrate.
  • Which type of enzyme is frequently composed of multiple subunits?

  • Hydrolases
  • Oxidoreductase
  • Allosteric enzymes (correct)
  • Transferases
  • What is the effect of phosphorylation on HMG-CoA reductase?

  • It is associated with serine or threonine residues only.
  • It increases the enzyme's activity. (correct)
  • It decreases the enzyme's activity.
  • It has no effect on the enzyme's activity.
  • Which of the following is an example of a ligase?

    <p>None of the above</p> Signup and view all the answers

    What is the effect of competitive inhibitors on the Michaelis constant?

    <p>They increase the Michaelis constant.</p> Signup and view all the answers

    What is the characteristic of an enzyme with high affinity for its substrate?

    <p>It has a low value of the Michaelis constant.</p> Signup and view all the answers

    What is the primary function of aminotransferases in cells?

    <p>To serve as an indicator of some diseases</p> Signup and view all the answers

    What does the Michaelis constant characterize?

    <p>The substrate specificity of an enzyme</p> Signup and view all the answers

    What is the role of enzymes in a reaction?

    <p>To decrease the energy barrier</p> Signup and view all the answers

    What type of catalysis involves the covalent bonding of the substrate to the enzyme?

    <p>Covalent catalysis</p> Signup and view all the answers

    What is the term for a molecule that binds to an enzyme and alters its activity?

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

    What is the term for multiple forms of an enzyme that have the same function but differ in their amino acid sequence?

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

    What is the effect of a noncompetitive inhibitor on the Michaelis constant?

    <p>It increases the Michaelis constant</p> Signup and view all the answers

    Which of the following statements is true about coenzyme A?

    <p>It is a carrier of acyl groups</p> Signup and view all the answers

    What is the characteristic of an enzyme that exhibits a Km value of 10^(-3)M?

    <p>Low substrate affinity</p> Signup and view all the answers

    What is the effect of an inhibitor on the kinetics of an enzymatic reaction, if Vmax is decreased and Km is unchanged?

    <p>Noncompetitive inhibition</p> Signup and view all the answers

    What is a characteristic of isozymes?

    <p>All of the above</p> Signup and view all the answers

    What is the effect of an enzyme on the standard Gibbs free energy change (ΔG0) of a reaction?

    <p>It has no effect on ΔG0</p> Signup and view all the answers

    Study Notes

    Enzyme Catalysis

    • Enzymes catalyze the joining of two molecules.
    • The Michaelis constant (Km) is a measure of the concentration of enzyme needed to achieve half of the maximal velocity of reaction.

    Enzyme Inhibition

    • Competitive inhibitors bind to the active site of the enzyme and do not change the Vmax of the reaction.
    • Noncompetitive inhibitors do not bind to the active site and decrease the Vmax of the reaction.

    Enzyme Structure

    • Lactate dehydrogenase (LDH) is composed of 4 subunits.
    • LDH isoenzymes catalyze different reactions in muscle and heart.

    Isozymes

    • Isozymes can have different Km for the same substrate.
    • Isozymes can have different isoelectric points.
    • LDH is coded by 4 genes and can form 5 isozymes.

    Enzyme Kinetics

    • Vmax is the maximum velocity of an enzymatic reaction.
    • Km is the Michaelis constant, which is a measure of the enzyme's affinity for its substrate.
    • The Michaelis constant can be affected by the presence of inhibitors.

    Types of Enzymes

    • Pepsin is a hydrolase.
    • Amylase is a hydrolase.
    • Aminotransferases are a type of transferase.
    • Oxidoreductases, transferases, hydrolases, isomerases, and lyases are all classes of enzymes.

    Allosteric Enzymes

    • Allosteric enzymes frequently contain multiple subunits.
    • Allosteric enzymes can be conformationally changed by allosteric effectors that alter Km or Vmax.

    Enzyme Regulation

    • Phosphorylation-dephosphorylation is associated with serine, threonine, or tyrosine residues of the enzyme.
    • HMG-CoA reductase is active in its dephosphorylated form.

    Clinical Enzymology

    • LDH activity in plasma can serve as an indicator of some diseases.
    • Aminotransferase activity in plasma can increase in pancreatic disease.
    • LDH activity in plasma can increase in myocardial infarction.

    Diagnosis

    • Measure LDH activity to diagnose myocardial infarction.
    • Measure aminotransferase activity to diagnose viral hepatitis.
    • Measure prostate-specific antigen (PSA) activity to diagnose metastatic carcinoma of the prostate.

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    Description

    Test your knowledge of biochemistry with this quiz on enzymes, coenzymes, and their roles in biochemical reactions. Questions cover topics like Michaelis constant, coenzyme A, and riboflavin.

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