Chapter 4
Enzymes and Energy
Chapter Scope
In the last chapter we learned about the amino acid composition and the structure of proteins. We also studied the process by which proteins are synthesized from information coded in the genes of the chromosomes. Perhaps the most important group of body proteins is that of enzymes — the subject of this chapter. These vital molecules act as biological catalysts, speeding up chemical reactions in such diverse regions of the body as in the stomach or in the intestine where powerful enzymes digest foods by hydrolysis (chapter 17), in the blood and kidney where the enzyme carbonic anhydrase helps maintain acid‑base balance (chapter 15), and within target cells where various enzymes activate second messenger systems in response to visiting hormones (chapter 11). Enzymes also serve as critical facilitators of cell respiration and other important metabolic pathways that take place in the cytoplasm and within the mitochondria of all cells to combust fuel molecules and provide energy for the cell's many activities (chapters 5, 18).
In the next chapter on cell metabolism, the enzymes introduced here will be appreciated as a specific enzyme catalyzes each step in the breakdown of fuel food molecules and the transfer of energy to adenosine triphosphate (ATP). Since enzymes are protein molecules assembled under the direction of the cell’s DNA, a single defective gene will result in the synthesis of a defective enzyme. Such defective enzymes can cause inborn errors of metabolism, which in severe cases may cause nervous system disorders or even death. Furthermore, the delicate tertiary structure of enzymes must be maintained so that the active site can receive substrate molecules during normal catalysis. Changes in acid‑base balance (such as acidosis or alkalosis) or variations in body temperature (such as hyperthermia or hypothermia) can disturb this precise protein architecture and interfere with the ability of enzymes to regulate metabolism.
With a job this vital to life, it is no wonder that enzymes recruit help from other molecules — namely, coenzymes and cofactors. In this chapter, we will be introduced to two important coenzymes, NAD and FAD, both derived from water‑soluble B vitamins. In similar fashion, these coenzymes function as carriers of hydrogen atoms, shuttling these atoms from place to place along metabolic pathways of the cell. In the next chapter on cell respiration, a third coenzyme (coenzyme A) is introduced that will join NAD and FAD in assisting the many metabolic enzymes working to extract and transfer energy from fuel foods to high‑energy ATP molecules.
I. Enzymes as Catalysts
Enzymes are biological catalysts that function to increase the rate of chemical reactions. Most enzymes are proteins, and their catalytic action results from their complex structure. The great diversity of protein structure allows different enzymes to be specialized in their action.
e. Enzymes often require the presence of minerals or other “helper” molecules.
II. Control of Enzyme Activity
The rate of an enzyme‑catalyzed reaction depends on numerous factors, including the concentration of the enzyme and the pH and temperature of the solution. Genetic control of enzyme concentration, for example, affects the rate of progress along particular metabolic pathways and thus regulates cellular metabolism.
e. Attachment of a phosphate group can inactivate certain zymogens.
e. All of these statements are true.
III. Bioenergetics
a. oxygen.
b. proton (H+).
c. electron (e-).
d. water.
e. ATP.
Chapter Review
Assume you have recently consumed a delicious cheeseburger as a source of body fuel. Also, assume that digestion and absorption into the body was successful such that simple sugars (like glucose) from carbohydrates, triglycerides from lipids, and amino acids from proteins are now present in your body cells. Here, the amino acids floating in the cytoplasm are used to make biological catalysts, or
55. ____________, as instructed by DNA. The various metal ions assist enzymes by working as
56. ____________, while the water‑soluble vitamins work primarily as 57. ____________. Under optimal conditions of 58. ____________and 59. ____________, enzymes can speed up the metabolism of your cheeseburger fuels, releasing 60. ____________from chemical bonds. Therefore, these reactions are
61. ____________ (endergonic/exergonic). The combustion of glucose as fuel in the cell results in the formation of 62. ____________and water; while some of the chemical‑bond energy is transferred to “high‑energy” bonds of 63. ____________or (____________), and the rest of the energy is lost as
64. ____________. The formation of this “universal energy carrier” is 65. ____________ (endergonic/exergonic), providing the cell with a usable form of energy.
In a similar fashion, triglycerides and amino acids can be combusted in the cell, transferring energy to power the cell's many energy‑requiring processes. Complete combustion of these fuels requires that we breathe so that blood can deliver the gas 66. ____________, which is the final electron 67. ____________ (acceptor/donor) in the cell. In the final step of metabolism, this gas is ultimately 68. ____________ (oxidized/reduced) to form 69. ____________.
Across
1. bioenergetics incorporates these first and second laws
3. the cell's “universal energy carrier”
7. reactions that require energy input
10. oxidizing or reducing ________
11. different model of the same enzyme
13. compounds mainly derived from water‑soluble vitamins
15. inborn error of phenylalanine (amino acid) metabolism
17. when an atom or molecule gains electrons
18. a new term, or number used to measure the ability of enzymes to convert substrates into products
20. an enzyme acts as a biological ________
21. an enzyme in blood/liver that breaks down hydrogen peroxide
23. a metal ion such as Ca2+, Mg2+, Mn2+, Cu2+, or Zn2+
24. the precise protein structure altered by pH and temperature
26. enzymes work by lowering the energy of ________
28. a unit of heat measurement
30. ________‑product inhibition
31. degree of disorganization or less free energy (hint: second law of thermodynamics)
Down
2. reactions that release energy
4. enzymes are most affected by pH and ________
5. biological catalyst described in this chapter
6. most metabolic pathways are not linear; rather they are ________
8. loss of electrons from an atom or molecule
9. the first law of thermodynamics conserves ________
12. the pigment missing in the albino due to a defective gene in DNA
14. also known as the reactant for enzyme‑catalyzed reactions
16. inborn errors of ________
19. a coenzyme derived from vitamin B2 (riboflavin)
22. energy that is organized and can be used to perform work
25. reversible chemical reactions must obey the law of ________ action
27. a hydrogen‑carrying coenzyme derived from niacin
29. the universal suffix for enzymes
32. all enzymes work best at their
optimal ________
This essay tutorial will answer the first essay question found in the “Review Activities,” section of your Human Physiology textbook. Read question 1 in the “Test Your Understanding of Concepts and Principles” section located at the end of chapter 4 and let me guide you through one possible answer. Watch for key terms in boldface type, helpful tips and general suggestions on writing the essay or short‑answer questions. Go ahead try this one, and a few of mine that follow!
70. Explain the relationship between an enzyme’s chemical structure and the function of the enzyme, and describe how both structure and function may be altered in various ways.
Answer. Most enzymes are proteins. Therefore enzymes exhibit primary, secondary, tertiary, and even quaternary structure. Since enzymes must bind to substrates with the three‑dimensional precision of a lock‑and‑key, any change in the enzyme (the lock) structure can interfere with binding by the substrate (the key).
Inborn errors of metabolism are inherited defects in the gene (DNA) which direct alterations of the enzyme’s primary structure (amino acid sequence) and, thus, can cause disease by reducing the activity or the “fit” between the substrate and the enzyme active site. In this way the tertiary structure (bending and folding) of the active site region of the enzyme determines its efficiency. Variation in both pH and temperature from some optimal value can distort or “warp” the delicate active site, reducing the “activity” of the enzyme and decreasing the number of products formed. Finally, the normal function of many enzymes requires the help of coenzymes and/or cofactors obtained from raw material such as vitamins and minerals, respectively. Consequently, a diet deficient in these raw materials can result in less productive enzyme‑catalyzed reactions.
71. Describe what is meant by the term “isoenzyme,” and include one example of an isoenzyme whose various forms rise abnormally high in the blood, thus aiding in the diagnosis of certain diseases. [Hint: see Table 4.1.]
72. Describe the variation in the pH experienced by your cheeseburger (from the Completion section) as it travels along the mouth, stomach, and small intestine (pancreas). From each of these locations, name one enzyme, state its optimal pH, and describe a reaction catalyzed by each enzyme.
[Hint: see Table 4.3.]
Note: These last two essay questions were written from information provided by tables — then, would it not make sense to answer each question using a similar table format? Try it!
73. Using phenylketonuria (PKU) as an example, explain how inborn errors of metabolism are inherited and describe how these errors can alter metabolism.
74. Explain the step‑by‑step processes that occur in the cytoplasm as the chemical‑bond energy in glucose is transferred to the “high‑energy” bonds of adenosine triphosphate (ATP).
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