Enzyme Overview and Nomenclature

1. Question 1
   • They can be denatured by alterations in pH or heat.
   • They lower the activation energy required for reactions.
   • They are composed of specific amino acid sequences.
   • They are consumed during the biochemical reaction.
2. Question 2
   • The abbreviated term widely used in laboratories.
   • The substrate acted upon, the reaction catalyzed, and any coenzymes.
   • A practical and easy name for laboratory use.
   • A four digit code and classification of the enzyme.
3. Question 3
   • Catalyzing hydrolysis of various bonds
   • Catalyzing the transfer of a group from one substrate to another
   • Catalyzing oxidation-reduction reactions
   • Catalyzing the removal of groups from substrates, resulting in double bonds
4. Question 4
   • Oxidoreductases
   • Hydrolases
   • Transferases
   • Isomerases
5. Question 5
   • Transferases
   • Isomerases
   • Lyases
   • Hydrolases
6. Question 6
   • The presence of cofactors.
   • The temperature of the reaction.
   • The concentration of the substrate.
   • The concentration of the enzyme.
7. Question 7
   • The temperature is too low.
   • The pH of the reaction is not optimal.
   • The enzyme is operating under first-order kinetics.
   • The enzyme is under saturated conditions.
8. Question 8
   • To ensure that the substrate does not deplete during the assay.
   • To maintain the enzyme in an unsaturated state.
   • To reduce the effects of temperature on the reaction rate.
   • To ensure the reaction follows first-order kinetics.
9. Question 9
   • The reaction rate will approximately double.
   • The reaction rate will approximately halve.
   • The reaction rate will approximately decrease by a factor of 4.
   • The reaction rate will approximately quadruple.
10. Question 10
    • A vitamin molecule.
    • A phosphate group.
    • A change in pH.
    • Magnesium ion ($Mg^{2+}$).
11. Question 11
    • They catalyze the breakdown of large molecules into smaller ones by adding water.
    • They catalyze the joining of two substrate molecules utilizing the energy from ATP hydrolysis.
    • They facilitate the transfer of functional groups between substrate molecules.
    • They induce oxidation-reduction reactions in substrate molecules.
12. Question 12
    • Enzymes are produced at higher than normal levels during healthy physiological processes.
    • Enzymes are always present in high concentrations in blood, so changes don't indicate disease.
    • Enzyme levels are normally low, so increased levels suggest cellular damage or leakage.
    • Enzymes only increase in the blood when there is too much substrate for them to act upon.
13. Question 13
    • All phases of the enzyme-catalyzed reaction.
    • Linear Phase, when product formation and substrate consumption are consistent.
    • Substrate Depletion Phase, when product formation slows.
    • Lag Phase, before equilibrium is reached.
14. Question 14
    • It requires multiple absorbance readings, increasing the time to perform the assay.
    • The readings may not be taken during the linear phase of the enzyme reaction.
    • It is unable to detect deviations from linearity.
    • It can only be used to measure one enzyme substrate at a time.
15. Question 15
    • Electrophoretic techniques because they measure isoenzymes or isoforms.
    • Immunoassays because they directly measure enzyme concentration by mass.
    • 2-Point Assay (Fixed time) because it's simpler to perform.
    • Kinetic Assay (Continuous Monitoring) because provides multiple absorbance readings.
16. Question 16
    • Apoenzyme
    • Coenzyme
    • Proenzyme/Zymogen
    • Holoenzyme
17. Question 17
    • When non-competitive inhibitors are present
    • First-order conditions with the enzyme in excess
    • First-order conditions with the substrate in excess
    • Zero-order conditions with the substrate in excess
18. Question 18
    • A coenzyme is always a vitamin, while a prosthetic group is not.
    • A coenzyme is loosely bound, while a prosthetic group is tightly bound.
    • A coenzyme is tightly bound, while a prosthetic group is not.
    • A coenzyme is inorganic, while a prosthetic group is organic.
19. Question 19
    • The reaction rate decreases as the substrate concentration increases.
    • The enzyme is the rate-limiting factor.
    • The reaction rate is proportional to the substrate concentration.
    • The reaction follows zero-order kinetics.
20. Question 20
    • The enzyme will catalyze the reaction of 250 μmol of substrate in 1 liter per minute.
    • The enzyme will catalyze the reaction of 1 μmol of substrate in 1 minute at 250 degrees Celsius.
    • The enzyme will catalyze the reaction of 250 mmol of substrate in 1 liter per minute.
    • The enzyme will catalyze the reaction of 1 μmol of substrate in 250 minutes per liter.

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