Enzymes and Their Properties

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Questions and Answers

What is the primary function of enzymes in a chemical reaction?

  • Increase the free energy of reactants
  • Convert substrates into products irreversibly
  • Change the equilibrium position of the reaction
  • Lower the energy barrier for the reaction (correct)

Which model of enzyme activity suggests that the active site undergoes a conformational change to fit the substrate?

  • Lock and key model
  • Static model
  • Dynamic model
  • Induced fit model (correct)

What aspect of the active site promotes high-affinity binding of a substrate?

  • Exclusion of all cofactors
  • Size and shape of the active site (correct)
  • Temperature of the reaction environment
  • Presence of only non-polar amino acids

How do enzymes lower the activation energy of a reaction?

<p>By inducing strain in substrate bonds (D)</p> Signup and view all the answers

What does the term 'proximity effect' refer to in enzyme catalysis?

<p>The spatial arrangement of substrates in the active site (B)</p> Signup and view all the answers

Which statement about enzymes is NOT true?

<p>They change the free energy of reactants (D)</p> Signup and view all the answers

What type of groups do enzymes provide that are critical for catalysis?

<p>Acidic, basic, or other types of groups (B)</p> Signup and view all the answers

Which of the following is NOT a property of the active site in enzymes?

<p>Contains every possible amino acid (D)</p> Signup and view all the answers

What role do isoenzymes play in response to cell signals?

<p>They may respond differently to specific cell signals due to regulatory properties. (A)</p> Signup and view all the answers

Which of the following is NOT a characteristic of all enzymes?

<p>They only work in aerobic conditions. (A)</p> Signup and view all the answers

What makes the CK2-MB isoenzyme useful as a diagnostic marker?

<p>It is unique to myocardial muscle and indicates specific damage. (C)</p> Signup and view all the answers

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

<p>To bind substrates and facilitate the reaction. (B)</p> Signup and view all the answers

Ribozymes are unique because they are composed primarily of which type of molecule?

<p>RNA. (B)</p> Signup and view all the answers

Which of the following correctly describes the formation of an enzyme-substrate complex?

<p>It forms transiently during the catalytic process. (D)</p> Signup and view all the answers

Which cofactor is typically associated with oxidative reactions?

<p>NAD+. (C)</p> Signup and view all the answers

What happens after the enzyme-substrate complex (ES) forms in the catalytic cycle?

<p>The substrate converts into product while still bound to the enzyme. (C)</p> Signup and view all the answers

What is one of the key components of the serine protease mechanism of catalysis?

<p>Tetrahedral oxyanion intermediate (B)</p> Signup and view all the answers

Which amino acids are primarily involved in the catalytic triad of serine proteases?

<p>Ser, His, and Asp (C)</p> Signup and view all the answers

Which factor does NOT affect enzyme catalytic activity?

<p>Color of the enzyme (D)</p> Signup and view all the answers

What effect does increasing temperature generally have on reaction rates?

<p>Increases reaction rates until denaturation occurs (A)</p> Signup and view all the answers

Which statement best describes the relationship between pH and enzyme activity?

<p>Every enzyme has a specific pH range for optimal activity (A)</p> Signup and view all the answers

What happens to the active site of an enzyme when the temperature is too high?

<p>It can denature and lose functionality (C)</p> Signup and view all the answers

What describes the effect of substrate concentration on the reaction rate of enzymes?

<p>Reaction rate increases with substrate concentration until saturation is reached (C)</p> Signup and view all the answers

Which of the following is a consequence of pH affecting enzymatic activity?

<p>Altered ionization states of amino acids (D)</p> Signup and view all the answers

Why is it essential for serine proteases to maintain a specific structural configuration?

<p>To facilitate efficient substrate binding and catalysis (A)</p> Signup and view all the answers

What is a characteristic of the optimum pH for an enzyme's activity?

<p>It varies among different enzymes (A)</p> Signup and view all the answers

What role do enzymes play in biochemical reactions?

<p>They act as biological catalysts. (B)</p> Signup and view all the answers

What is the impact of enzymes on reaction rates?

<p>They increase reaction rates by a factor of up to about 1014 to 1016. (B)</p> Signup and view all the answers

Which statement about enzyme consumption in reactions is true?

<p>Enzymes are not consumed during the course of the reaction. (D)</p> Signup and view all the answers

What are cofactors in relation to enzymes?

<p>Cofactors may be inorganic ions, coenzymes, or organometallic groups. (A)</p> Signup and view all the answers

What happens to enzyme activity when its structure is denatured?

<p>Enzyme activity is decreased or destroyed. (A)</p> Signup and view all the answers

Which of the following statements about enzyme localization is accurate?

<p>Enzymes in the same metabolic pathways are often compartmentalized together. (C)</p> Signup and view all the answers

How do cofactors influence enzyme functions besides catalysis?

<p>They can influence the enzyme's tertiary structure. (A)</p> Signup and view all the answers

What is the difference between an apoenzyme and a holoenzyme?

<p>An apoenzyme is an enzyme without a cofactor, while a holoenzyme includes the cofactor. (B)</p> Signup and view all the answers

What does one International Unit (IU) of an enzyme represent?

<p>The amount that catalyzes the formation of one micromole of product in one minute (C)</p> Signup and view all the answers

How is specific activity defined?

<p>Units of enzyme activity per milligram of protein (C)</p> Signup and view all the answers

What happens to specific activity after purification of an enzyme?

<p>It increases as the enzyme becomes more pure (A)</p> Signup and view all the answers

How is enzyme activity affected by changes in environmental conditions?

<p>Enzyme activity is sensitive to pH, temperature, and ionic strength (A)</p> Signup and view all the answers

Why might a low activity enzyme require more total amount for the same reaction rate as a high activity enzyme?

<p>To compensate for the slower reaction rate of low activity enzymes (C)</p> Signup and view all the answers

What is an isoenzyme?

<p>A different form of an enzyme that catalyzes the same reaction (D)</p> Signup and view all the answers

Which of the following statements is true regarding the relationship between total amount of enzyme and specific activity?

<p>Low total amount of enzyme can indicate higher specific activity (C)</p> Signup and view all the answers

In order to express enzyme activity, which of the following is crucial to denote?

<p>The specific assay conditions used (C)</p> Signup and view all the answers

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Study Notes

Enzymes

  • Proteins that act as biological catalysts.
  • Accelerate reaction rates for up to 10^14 to 10^16 times.
  • Reduce or prevent generation of unwanted by-products.
  • Work in an organized sequence to produce specific products.
  • Not consumed during the reaction.
  • Cannot change the free energy of a reaction.

Enzyme Properties

  • Molecular weight ranges from 12,000 to over 1 million Da.
  • Requires native protein conformation for catalytic activity.
  • Localization is important, with enzymes within the same pathways often compartmentalized together.
  • Compartmentalized to prevent unwanted activity.

Cofactors

  • Additional components required for catalytic activity.
  • Include inorganic ions, coenzymes, and organometallic groups.
  • Apoenzyme + cofactor = holoenzyme.
  • Assist in reactions by forming covalent interactions with substrate.
  • Oxidation-reduction with unique functional groups that accept or donate electrons.
  • Can influence enzyme tertiary structure.

Measuring Enzyme Activity

  • One International Unit (IU):
    • The amount of enzyme that catalyzes the formation of one micromole of product in one minute (1 U = μmol/min).
    • Conditions of the assay must be specified because enzymes are sensitive to pH, temperature, and ionic strength.
  • Specific activity:
    • Units of enzyme activity per milligram of protein in a sample.
    • A measure of enzyme purity.

Isoenzymes

  • Different forms of an enzyme that catalyze the same chemical reaction.
  • May vary in:
    • Sub-cellular location.
    • Tissue distribution.
    • Kinetic properties (affinity for substrates and inhibitors, regulatory properties, and cofactors used).
  • Can be useful diagnostic markers for tissue damage.

Creative Kinase (CK) Isoenzymes

  • Found in different tissues:
    • CK1 – BB (brain).
    • CK2 – MB: (cardiac).
    • CK3 – MM: (muscle).
  • Measured in blood to diagnose tissue damage
    • Elevated CK2-MB levels suggest heart damage.
    • Skeletal muscle and brain have different isoforms.

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