CHAPTER 4 ENZYMES

1. What are enzymes?

2. Are enzymes globular or fibrous?
3. Define catalysts.
4. Define substrate.
5. Define product.
6. What is meant by turnover number?
7. How are biological catalysts/enzymes different to chemical catalysts and why is this
important for living organisms?
8. What is activation energy and how do enzymes affect this energy?
9. Describe two ways in which an enzyme can lower activation energy.
ENZYME STRUCUTURE DETERMINES FUNCTION
10. Where are the instructions for making enzymes found- how can this lead to a change
in the structure of enzyme?
11. What are cofactors?
12. What happens if an enzyme is deficient?
13. Define active site.
14. Explain why enzymes are highly specific (active site and T.S)
15. How can changes in environment cause a change in active site?
16. What are intracellular enzymes?
17. What are extracellular enzymes?
18. What is a metabolic pathway?
19. What are metabolites?
20. Define metabolism.
21. What is a catabolic pathway?
22. Define catabolism.
23. What is an anabolic pathway?
24. Define anabolism.
25. What is required for anabolism to occur?
26. Name 2 complex metabolic pathway in living OG.
27. How can one enzyme stop the entire metabolic pathway from running?
28. What is catalase?
29. Is catalase intracellular or extracellular?
30. Describe the structure of catalase.
31. Where is catalase found in eukaryotic cells?
32. How is catalase used by WBCs?
33. What is the optimum pH of catalase in humans vs other organisms?
EXTRACELLULAR ENZYMES
34. Use fungi as an example to describe how extracellular enzymes work.
35. Give an example of extracellular enzymes in humans.
36. What is amylase?
37. Where is amylase produced?
38. Describe the 2-step process by which starch is digested and name the 2 enzymes
involved.
39. What is trypsin and where is it produced?
40. What role does it carry out and at what pH?
41. Where are most digestive enzymes released from in humans?
42. What do these enzymes do?
43. Where are the products of digestion absorbed?

2.4.2-COFACTORS (good notes in cgp guide)

1. Define cofactor.
2. What is a prosthetic group?
3. Are prosthetic groups organic or inorganic?
4. What bonds form between enzyme and prosthetic group?
5. Name the prosthetic group found in carbonic anhydrase.
6. What is the role of carbonic anhydrase and where is it found?
7. Why is the reaction catalysed by carbonic anhydrase important?
8. Define enzyme substrate complex.
9. What are co-substrates?
10. What are inorganic cofactors and what is their role?
11. Do inorganic cofactors change by the end of a reaction?
12. What ion must be present for amylase to function? (what type of cofactor is this?)
13. Define coenzyme?
14. Do coenzymes bind temporarily or permanently?
15. When do coenzymes bind to the enzyme?
16. What happens to a coenzyme during a reaction?
17. Where are most coenzymes derived from?
18. Which coenzyme is derived from vitamin B12?
19. What would happen if a human were vitamin B-12 deficient?

20. Which coenzyme is derived from folic acid (vitamin) and what if someone were folic
acid deficient?
21. Which coenzyme is derived from Thiamine, B1?
22. What would a deficiency of thiamine B1 cause?
23. Where are NAD and NADP derived from? What do they accept?
KERBOODLE-Precursor activation:
24. What is an inactive precursor enzyme?
25. How are precursor enzymes activated (3 ways)?

26. What are apoenzyme and holoenzyme?

27. What are proenzymes/zymogens?
28. What is pepsin celled before activated?
29. Describe the activation of pepsinogen and why it is essential for it to only become
active in stomach?
NOTES:
 Think as: 2 types of cofactors- inorganic cofactors (could be inorganic molecules
or inorganic ions) and organic cofactors (coenzymes).
 If cofactor (organic or inorganic) is tightly and permanently bound to enzyme it is
a prosthetic group.
 Co-substrate -> they and the substate together form the correct shape to bind to
active site.

2.4.3 Mechanism of enzyme action

LOCK AND KEY HYPOTHESIS
 1. Define enzyme-substrate complex.
2. Define enzyme-product complex.

3. Describe the active site and substrate molecule structure in lock and key model?
4. Describe the process of a lock and key model.
5. What 2 things can happen to substrate molecules in the active site?
6. Describe the active site of enzyme after products leave?
INDUCED FIT HYPOTHESIS
7. Why is the lock and key hypothesis not a very good model?
8. In contrast, why may the lock and key hypothesis be described as a good model.
9. What is the theory behind the induced fit hypothesis (what does it suggest)?
10. Describe the process by which an enzyme catalyses a reaction using induced fit
hypothesis.
11. What types of forces bind the substrate molecule to active site?
12. Why do product molecules leave?
13. How is the induced fit hypothesis different to lock and key hypothesis?
ACTIVATION ENERGY
14. What is required for chemical reactions to begin?
15. How can activation energy be provided to chemical reactions?
16. Why can’t the same method be applied to living cells? (what happens to proteins
and lipids)
17. How do enzymes lower activation energy?

2.4.4 Temperature affecting enzyme activity

1) Define denatured.
2) What happens if the reaction mixture containing enzyme and substrate molecule is
heated?
3) Define optimum temperature.
4) Other than making molecules move faster what else can increasing the temperature
further do?
5) What type of bonds in the active site of enzyme may break on increasing temp?
6) What happens when reaction mixture is heated above optimum temperature?
7) Why is the primary structure un-altered when enzyme denatures?
8) Why does the rate of reaction fall above optimum temperature?
9) Describe the process of denaturation.

OPTIMUM TEMPERATURE
10) Describe the optimum temperature of enzymes of organisms adapted to cold
environments.
11) Describe the optimum temperatures of enzymes of organisms adapted to hot
environments.
a) What type of bonds are present (in larger amounts)?
12) Draw and ANNOTATE a graph of the effect of temperature on an enzyme catalysed
reaction.
13) How do you calculate rate of reaction + units?
14) What is the optimum temperature of most enzymes in a human body?
TEMPERATURE COEFFIECIENT Q10
15) Define Q10
16) What is the temperature coefficient of enzyme catalysed reactions?
17) What is the equation of Q10?
18) Why is the temperature coefficient 2 for enzyme substrate molecules?
19) What happens to temperature coefficient above optimum temperature? Explain why.
20) Explain why an enzyme solution kept in fridge will catalyse a reaction at 40C but a
enzyme solution boiled does not.

2.4.5 pH and ENZYME ACTIVITY

1) What is pH?
2) What do different pH values indicate?
3) What are acids?
4) What is a buffer?
5) How is the pH of blood kept close to 7.4? Why?
6) How is pH worked out? What does high acidity mean in terms of pH?
7) What is a hydrogen ion?
8) Explain how protons/hydrogen ions interfere with hydrogen bonds holding the tertiary
structure of enzyme.
9) What happens to shape of enzyme molecule when excess hydrogen ions interfere with
hydrogen bonds and ionic forces?
10) How does increasing hydrogen ion concentration affect charges on active site?
11) What is optimum pH?
12) What happens to enzyme activity when small changes to pH are made either side of
optimum? Why?
13) What would happen if normal optimum temperature is restored? Why?
14) Define renaturation.
15) When will the enzyme become denatured and what effect does this have on rate of
reaction?
16) Draw and ANNOTATE a graph showing rate of reaction against pH.
NOT ALL ENZYMES HAVE SAME OPTIMUM pH
17) What is the pH of intracellular enzymes?
18) What is the optimum pH of amylase (in first part of digestion in mouth)?
19) What is the optimum pH of protease-pepsin?
i) Why (where are they found)?
ii) What is the role of hydrochloric acid in stomach?
iii) What is the role of pepsin?
20) What is the optimum pH of protein-digesting enzymes e.g., trypsin?
i) Where are these found?
ii) Why is the pH in small intestine higher than in stomach?
iii) What is the role of trypsin?

2.4.6 SUBSTRATE CONC. AND RATE OF REACTIONS

1. Define concentration.
2. What would happen to an enzyme catalysed reaction if no substrate is present?
 3. What happens to rate of reaction as substrate conc. increases?
(a) Why?
(b) What is the limiting factor in this situation?
(c) What is a limiting factor?
2) What would happen if the substrate concentration is increased further?
i) Why?
ii) Draw and ANNOTATE a graph showing initial rate of reaction against substrate
concentration.
iii) What is the limiting factor when graph plateaus?
3) What is the Vmax?
4) How can rate of reactivity be increased at the Vmax?

2.4.7 ENZYME CONCENTRATION AND RATE OF REACTION

1. What does enzyme availability/concentration depend on?

2. What controls these rates?
3. How does cell control enzyme synthesis?
4. What happens in enzyme degradation?
5. State 2 advantages of degrading enzymes and synthesising new proteins from amino
acids?
6. What is the source of amino acids for enzymes that have not come form
degradation? (pearson)
7. What happens to the rate of reaction as enzyme concentration increases?
8. What is the limiting factor in this case?
9. What would happen if the enzyme concentration is increased further (at a fixed
substrate concentration)?
10. Wat is the limiting factor now? Why?
11. Draw and ANNOTATE a graph of initial rate of reaction and enzyme concentration.

INITIAL RATE OF REACTION

12. Why is the initial rate of reaction the fastest for all enzyme catalysed reactions?
13. How can you calculate the initial rection rate from a graph?
14. Suggest why number of enzyme molecules within living cells is kept relatively low
(Pearson).

2.4.8 ENZYME INHIBITORS

1. Define competitive inhibition.
2. Define non-competitive inhibition.
3. What is the ‘goal” of inhibitor molecule (regardless of competitive or non
competitive)?
4. Define inhibitor.
5. How can inhibitors reduce enzyme activity- 2 ways?

COMPETITIVE INHIBITORS
6. What are competitive inhibitors?
7. Does competitive inhibition change the Vmax? Why?
8. How does a competitive inhibitor reduce enzyme activity/ rate of reaction?
9. What does the amount of inhibition depend upon?
10. What would happen when relative concentration of inhibitors is increased/ when
relative concentration of substrates in increased?
11. What complex do inhibitors form with enzyme?
12. Is enzyme inhibition by competitive inhibitors reversible?
13. How can the reaction be reversed?
14. What is meant by an inactivator?
15. Draw a graph of initial rate of reaction against substrate concentration with and
without competitive inhibitor?
16. What word is used to describe a reaction between enzyme and inhibitor (when
enzyme inhibitor complex forms)?

NON-COMPETITIVE INHIBITION
17. Where do non-competitive inhibitors bind?
18. How are non-competitive inhibitors different to competitive inhibitors?
19. Define allosteric site.
20. What affect does the binding of inhibitor to allosteric site have on enzyme?
21. Do non-competitive inhibitors affect Vmax/ maximum rate of reaction? Explain why?
22. How does the concentration of non-competitive inhibitors affect enzyme activity?
23. Are non-competitive inhibitors reversible?
24. What type of bonds form between inhibitor and enzyme during reversible inhibition?
25. What type of bonds form between inhibitor and enzyme during irreversible
inhibition?

END PRODUCT INHIBITON

26. What is end-product inhibition?
27. What is this regulation an example of?
28. Why is end product inhibition useful?
29. State and describe 2 ways in which end product inhibition may occur?
30. Explain how end product inhibition works to regulate/control metabolic pathways?
31. Is the competitive inhibition in a metabolic sequence reversible? Why?
32. How do multi-enzyme complexes increase the efficiency of metabolic reactions?
33. How can you differentiate between competitive vs non-competitive inhibition based
on graph AND by increasing substrate concentration?
34. What is a metabolic pathway?

2.4.9 ENZYME INHIBITION- POISONS AND MEDICINAL DRUGS

METABOLIC POISONS as enzyme inhibitors
1. What is the difference between venom and poison?
2. Why is KCN toxic (2 ways)?
3. How does KCN inhibit aerobic respiration?
4. Is cyanide a competitive/non competitive and reversible/irreversible inhibitor?
5. Why is the green mamba snake venom toxic?
6. How does snake venom (green mamba) cause paralysis?
7. What does ACh remain attached to?
8. What would happen if breathing muscles are paralysed?

MEDICINAL DRUGS ACTING BY INHIBITING ENZYMES

9. What is aspirin used for?

10. Which substance in aspirin carries out inhibition?
11. What do prostaglandins do?
12. How does aspirin relieve pain?
13. Other than pain relief, what is aspirin used for?
14. What are ATPase inhibitors used to treat?
15. What do ATPase inhibitors inhibit (not ATP)?
16. How do they affect the heart and treat heart failure?
17. What are protease inhibitors used to treat?
18. What type of inhibition do they use?
19. What are they competing with?
20. How do they treat viral infections?