Microbiology with Diseases by Body System (5th Edition)
5th Edition
ISBN: 9780134477206
Author: Robert W. Bauman Ph.D.
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 4SA
How does a nor-competitive inhibitor at a single allosteric site affect a whole pathway of enzymatic reactions?
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What roles do proximity and orientation play in enzymatic catalysis?
When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?
All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.
Chapter 5 Solutions
Microbiology with Diseases by Body System (5th Edition)
Ch. 5 - How can oxidation take place in an anaerobic...Ch. 5 - Why do electrons carried by NADH allow for...Ch. 5 - Why does catabolism of amino acids for energy...Ch. 5 - An uninformed student describes the Calvin-Benson...Ch. 5 - Prob. 5TMWCh. 5 - Why is feedback inhibition necessary for...Ch. 5 - Breaks a large molecule into smaller ones a....Ch. 5 - Includes dehydration synthesis reactions a....Ch. 5 - Prob. 3MCCh. 5 - Prob. 4MC
Ch. 5 - Involves the production of cell membrane...Ch. 5 - Includes hydrolytic reactions a. anabolism only b....Ch. 5 - Includes metabolism a. anabolism only b. both...Ch. 5 - Prob. 8MCCh. 5 - A reduced molecule _________. a. has gained...Ch. 5 - Prob. 10MCCh. 5 - Coenzymes are ________. a. types of apoenzymes b....Ch. 5 - Which of the following statements best describes...Ch. 5 - Which of the following does not affect the...Ch. 5 - Most oxidation reactions in bacteria involve the...Ch. 5 - Under ideal conditions, the fermentation of one...Ch. 5 - Under ideal conditions, the complete aerobic...Ch. 5 - Which of the following statements about the...Ch. 5 - Reactions involved in the light-independent...Ch. 5 - The glycolysis pathway is basically __________. a....Ch. 5 - A major difference between anaerobic respiration...Ch. 5 - 1. _______ Occurs when energy from a compound...Ch. 5 - Fill in the Blanks 1. The final electron acceptor...Ch. 5 - Fill in the Blanks 2. Two ATP molecules are used...Ch. 5 - Fill in the Blanks 3. The initial catabolism of...Ch. 5 - Fill in the Blanks 4. ________ is a cyclic series...Ch. 5 - Fill in the Blanks 5. The final electron acceptor...Ch. 5 - Fill in the Blanks 6. Three common inorganic...Ch. 5 - Fill in the Blanks 7. Anaerobic respiration...Ch. 5 - Fill in the Blanks 8. Complete the following...Ch. 5 - Prob. 9FIBCh. 5 - Fill in the Blanks 10 The main coenzymes that...Ch. 5 - VISUALIZE IT! 1 Label the mitochondrion to...Ch. 5 - Label the diagram below to indicate acetyl-CoA,...Ch. 5 - Examine the biosynthetic pathway for the...Ch. 5 - Prob. 1SACh. 5 - Why we enzymes necessary for anabolic reactions to...Ch. 5 - How do organisms control the rate of metabolic...Ch. 5 - How does a nor-competitive inhibitor at a single...Ch. 5 - Explain the mechanism of negative feedback with...Ch. 5 - Facultative anaerobes can live under either...Ch. 5 - How does oxidation of a molecule occur without...Ch. 5 - List at least four groups of microorganisms that...Ch. 5 - Why do we breathe oxygen and give of carbon...Ch. 5 - Why do cyanobacteria and algae take in carbon...Ch. 5 - What happens to the carbon atoms in sugar...Ch. 5 - How do yeast cells make alcohol and cause bread to...Ch. 5 - Where specifically does the most significant...Ch. 5 - Why are vitamins essential metabolic factors for...Ch. 5 - A laboratory scientist notices that a cer1ain...Ch. 5 - Arsenic is a poison that exists in two states in...Ch. 5 - Explain why an excess of all three of the amino...Ch. 5 - Why might an organism that uses glycolysis and the...Ch. 5 - Describe how bacterial fermentation causes milk to...Ch. 5 - Giardia intestinalis and Entamoeba histolytica are...Ch. 5 - Two cultures of a facultative anaerobe are grown...Ch. 5 - What is the maximum number of molecules of ATP...Ch. 5 - In terms of its effects on human metabolism, why...Ch. 5 - Cyanide is a potent poison because it irreversibly...Ch. 5 - How are photophosphorylation and oxidative...Ch. 5 - Members of the pathogenic bacterial genus...Ch. 5 - Compare and contrast aerobic respiration,...Ch. 5 - Scientists estimate that up to one-third of Earths...Ch. 5 - A young student was troubled by the idea that a...Ch. 5 - If a bacterium uses beta-oxidation to catabolize a...Ch. 5 - Some desert rodents rarely have water to drink....Ch. 5 - Prob. 17CTCh. 5 - We have examined the total ATP, NADH, and FADH2...Ch. 5 - Explain why hyperthermophiles do not cause disease...Ch. 5 - In addition to extremes in temperature and pH,...Ch. 5 - Figure 5.18b illustrates events in aerobic...Ch. 5 - Suppose you could insert a tiny pH probe into the...Ch. 5 - Even though Pseudomonas aeruginosa and...Ch. 5 - Photosynthetic organisms are rarely pathogenic....Ch. 5 - Prob. 25CTCh. 5 - A scientist moves a green plant grown in sunlight...Ch. 5 - What class of enzyme is involved in amination...Ch. 5 - Using the following terms, fill in the following...
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- Are enzyme-catalyzed reactions examples of homogeneous or heterogeneous catalysis?arrow_forwardThe active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?arrow_forwardWhat is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?arrow_forward
- For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?arrow_forwardWhat are the three most common mechanisms for enzymecatalyzed reactions that have two substrates?arrow_forwardIn what way is the observed mode of action of hexokinase consistent with the induced-fit theory of enzyme action?arrow_forward
- What is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?arrow_forwardWhat does it mean to say that an enzyme- catalyzed reaction is either enzyme limited or substrate -limited?arrow_forwardWhen enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substratesarrow_forward
- You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non- ionizable R groups.A) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate ending your answer with the product and free enzyme.arrow_forwardYou have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new enzyme uses the same catalytic triad and the same reaction mechanism as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups. a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product and free enzyme. b) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s)., Ser lle Zn Val c) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate of your new.enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows…arrow_forwardWhen enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.arrow_forward
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