Microbiology With Diseases By Taxonomy (6th Edition)
6th Edition
ISBN: 9780134832302
Author: Robert W. Bauman Ph.D.
Publisher: PEARSON
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Chapter 5, Problem 4SA
Summary Introduction
To determine:
The way in which a non competitive inhibitor at a single allosteric site affect a whole pathway of enzymatic reactions.
Introduction:
In a
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Chapter 5 Solutions
Microbiology With Diseases By Taxonomy (6th Edition)
Ch. 5 - How can oxidation take place in an anaerobic...Ch. 5 - Prob. 2TMWCh. 5 - Prob. 3TMWCh. 5 - Prob. 4TMWCh. 5 - Prob. 5TMWCh. 5 - Prob. 6TMWCh. 5 - Prob. 1MCCh. 5 - Prob. 2MCCh. 5 - Prob. 3MCCh. 5 - Prob. 4MC
Ch. 5 - Prob. 5MCCh. 5 - Prob. 6MCCh. 5 - Prob. 7MCCh. 5 - Prob. 8MCCh. 5 - Prob. 9MCCh. 5 - Prob. 10MCCh. 5 - Prob. 11MCCh. 5 - Prob. 12MCCh. 5 - Prob. 13MCCh. 5 - Prob. 14MCCh. 5 - Prob. 15MCCh. 5 - Prob. 16MCCh. 5 - Prob. 17MCCh. 5 - Prob. 19MCCh. 5 - Prob. 20MCCh. 5 - Prob. 1MCh. 5 - Prob. 1FIBCh. 5 - Prob. 2FIBCh. 5 - Prob. 3FIBCh. 5 - Prob. 4FIBCh. 5 - Prob. 5FIBCh. 5 - Prob. 6FIBCh. 5 - Prob. 7FIBCh. 5 - Prob. 8FIBCh. 5 - Prob. 9FIBCh. 5 - Prob. 10FIBCh. 5 - Examine the biosynthetic pathway for the...Ch. 5 - Prob. 1SACh. 5 - Prob. 2SACh. 5 - Prob. 3SACh. 5 - Prob. 4SACh. 5 - Prob. 5SACh. 5 - Prob. 6SACh. 5 - Prob. 7SACh. 5 - Prob. 8SACh. 5 - Prob. 9SACh. 5 - Prob. 10SACh. 5 - Prob. 11SACh. 5 - Prob. 12SACh. 5 - Prob. 13SACh. 5 - Prob. 14SACh. 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 - Describe how bacterial fermentation causes milk to...Ch. 5 - Giardia intestinalis and Entamoeba histolytica are...Ch. 5 - Prob. 6CTCh. 5 - Prob. 7CTCh. 5 - Prob. 8CTCh. 5 - Cyanide is a potent poison because it irreversibly...Ch. 5 - How are photophosphorylation and oxidative...Ch. 5 - Prob. 11CTCh. 5 - Compare and contrast aerobic respiration,...Ch. 5 - Scientists estimate that up to one-third of Earths...Ch. 5 - Prob. 14CTCh. 5 - Prob. 15CTCh. 5 - Some desert rodents rarely have water to drink....Ch. 5 - Prob. 17CTCh. 5 - Prob. 18CTCh. 5 - Explain why hyperthermophiles do not cause disease...Ch. 5 - In addition to extremes in temperature and pH,...Ch. 5 - Prob. 21CTCh. 5 - Prob. 22CTCh. 5 - Prob. 23CTCh. 5 - Prob. 24CTCh. 5 - Prob. 25CTCh. 5 - A scientist moves a green plant grown in sunlight...Ch. 5 - What class of enzyme is involved in amination...
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- 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.arrow_forwardAre enzyme-catalyzed reactions examples of homogeneous or heterogeneous catalysis?arrow_forwardFor 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_forward
- What is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?arrow_forwardWhat are the three most common mechanisms for enzymecatalyzed reactions that have two substrates?arrow_forwardWhat is the relative inhibition of an enzyme by a competitive inhibitor at [S] = KS and [I] = KI?arrow_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 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 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_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 the product and free enzyme.arrow_forward
- What does it mean to say that an enzyme- catalyzed reaction is either enzyme limited or substrate -limited?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 the 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 ile Zn+ Val C) You've constructed a molecule that is able to bind to the 1st 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_forwardWhat is the difference between competitive and non-competitive inhibition?arrow_forward
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