Prescott's Microbiology
10th Edition
ISBN: 9781259281594
Author: Joanne Willey, Linda Sherwood Adjunt Professor Lecturer, Christopher J. Woolverton Professor
Publisher: McGraw-Hill Education
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Chapter 10.6, Problem 2MI
Summary Introduction
To explain: The notion of a minimum inhibitory concentration of sulfanilamide.
Introduction: Pathogenic microorganisms can be poisoned by enzyme inhibitors. Competitive inhibitors resemble substrates and thus compete with the substrate for the catalytic site of the enzyme. This prevents the enzyme from making products.
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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.
For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absence of the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.
(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.
Chapter 10 Solutions
Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - What kinds of work are carried out in a cell?...Ch. 10.1 - What is thermodynamics? Summarize the first and...Ch. 10.1 - Define entropy and enthalpy. Do living cells...Ch. 10.1 - Prob. 4RIACh. 10.1 - Prob. 5RIACh. 10.2 - Why is ATP called a high-energy molecule? How is...Ch. 10.2 - Describe the energy cycle and ATPs role in it....Ch. 10.3 - Prob. 1MICh. 10.3 - Prob. 2MI
Ch. 10.4 - Figure 10.6 Electron Movement and Reduction...Ch. 10.4 - How is the direction of electron flow between...Ch. 10.4 - When electrons flow from the NAD+/NADH conjugate...Ch. 10.4 - Which among the following would be the best...Ch. 10.4 - In general terms, how is G related to E0? What is...Ch. 10.4 - Name and briefly describe the major electron...Ch. 10.6 - Will an enzyme with a relatively high Km have a...Ch. 10.6 - Prob. 2MICh. 10.6 - What is an apoenzyme? A holoenzyme? What are the...Ch. 10.6 - Illustrate the effect enzymes have on the...Ch. 10.6 - How does enzyme activity change with substrate...Ch. 10.6 - What special properties might an enzyme isolated...Ch. 10.6 - What are competitive and noncompetitive...Ch. 10.6 - How are enzymes and ribozymes similar? How do they...Ch. 10.7 - Figure 10.19 Allosteric Regulation. The structure...Ch. 10.7 - Figure 10.21 Feedback Inhibition. Feedback...Ch. 10.7 - Briefly describe the three ways a metabolic...Ch. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 4RIACh. 10.7 - Prob. 5RIACh. 10.7 - What is the significance of the fact that...Ch. 10 - Examine the structures of macromolecules in...Ch. 10 - Most enzymes do not operate at their biochemical...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 4CHI
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- Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)arrow_forwardHow does enzyme inhibition occur? Give and illustrate the reaction between enzyme and substrate in three types of enzyme inhibition. Also explain briefly the importance of enzyme inhibition in biochemistry.arrow_forwardThe same enzyme as studied in the presence of a different inhibitor (inhibitor B). In this case, two different concentrations of inhibitor are used. Data are as follows: (a) What kind of inhibitor is inhibitor B?(b) Determine the apparent Vmax and KM at each inhibitor concentration.(c) Estimate K1 from these data.arrow_forward
- b) Enzymes accelerate reactions by facilitating the formation of the transition state. Define transition state and activation energy. For full credit, you need to present the actual graph (for an endergonic or exergonic reaction - make sure to specify your choice) highlighting each term? c) Explain how an irreversible inhibitor for an enzymatic reaction differs from reversible inhibitors. Provide specific example of an irreversible inhibitor and its target enzyme d) Determine the Vo as a function of Vmax when the substrate concentration is equal to 10 KM or 20 KM. What does this tell you about an enzyme ability to reach Vmax?arrow_forwardA generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.arrow_forwardOnly a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.arrow_forward
- Hand written solutions are strictly prohibited.arrow_forward(a) Fill in the blank regarding the mechanism of chymotrypsin below. (1) Polypeptide substrate binds non covalently in the enzyme active site. The catalytic Triad includes a reactive Nucleophile that attacks the electrophilic amide C atom. (2) The resulting tetrahedral - Is stabilized by H-bonding interactions with the hole.(Note: this is the same word repeated) (3) Collapse of the tetrahedral intermediate and H * Transfer from- Lead to the Cleavage of the C-N bond. The N-terminal peptide is bound through acyl linkage to serine. (4) A Molecule then binds to the active site and attacks the acyl ester car- bonyl. (5) The resulting tetrahedral Tions with the Same word repeated). (6) The second peptide fragment is released, and the enzyme returns to its initial state. Intermediate is stabilized via enthalpic interac- hole. (Note: this is the same answer as (2), and is again the (b) Trypsin and chymotrypsin are two closely related proteases; however, trypsin cleaves after positively charged…arrow_forwardPlease fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis.arrow_forward
- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.arrow_forward(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?arrow_forwardChemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O Falsearrow_forward
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