Prescott's Microbiology
11th Edition
ISBN: 9781260211887
Author: WILLEY, Sandman, Wood
Publisher: McGraw Hill
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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.
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)
Chapter 10 Solutions
Prescott's Microbiology
Ch. 10.1 - Figure 10.2 The Relationship of G to the...Ch. 10.1 - Prob. 1CCCh. 10.1 - Prob. 2CCCh. 10.1 - Prob. 3CCCh. 10.1 - Prob. 4CCCh. 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. 2MICh. 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 - Prob. 1CCCh. 10.6 - Prob. 2CCCh. 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 - Prob. 2MICh. 10.7 - Define the terms metabolic channeling and...Ch. 10.7 - Define allosteric enzyme and allosteric effector.Ch. 10.7 - Prob. 3CCCh. 10.7 - Prob. 4CCCh. 10.7 - Prob. 5CCCh. 10 - Prob. 1RCCh. 10 - Prob. 2RCCh. 10 - Prob. 3RCCh. 10 - Examine the structures of macromolecules in...Ch. 10 - Examine the branched pathway shown here for the...Ch. 10 - Prob. 3AL
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- How 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_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_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_forwardIdentify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.arrow_forward
- Chemical 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_forwardBecause it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?arrow_forwardDescribe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..arrow_forward
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