Connect With Learnsmart Labs Online Access For Prescott's Microbiology
11th Edition
ISBN: 9781260408997
Author: Joanne Willey
Publisher: Mcgraw-hill Higher Education (us)
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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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The following statements refer to enzyme inhibition. Match the statement to the one of
the following descriptors to which it is best associated.
Descriptors: competitive inhibition; non-competitive inhibition; un-competitive; covalent
inhibition.
9a. Inhibition is not reversed even after the inhibitor (1) is removed from solution by
dialysis or drug metabolism/excretion.
9b. Inhibitor and substrate reversibly compete for occupancy of a common binding site
9c. The inhibitor binds reversibly only to the preformed E.S (enzyme-substrate) complex
forming an inactive E.S.I.
9d. The inhibitor binds reversibly and independently of substrate to an allosteric site
producing E.I or a ternary E.S.I complex which can't form product.
9f. The relative amount of inhibition decreases as [S] (the concentration of substrate)
increases and S better competes for occupancy of the active site.
The 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.
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
Connect With Learnsmart Labs Online Access For 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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- 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_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_forward
- Only 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(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.arrow_forwardDrug D reversibly binds to enzyme E and inhibits its activity toward substrate S. D binds equally well whether or not S is bound. Sketch a graph of the expected 1/v vs. 1/[S] relationship for: A) The enzyme reacting with S in the absence of drug D, B) The enzyme reacting with S in the presence of a small amount of drug D, and C) The enzyme reacting with S in the presence of a large amount of drug D.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_forwardExplain the biochemical basis of how temperature and pH affect enzyme activity. What are the changes in the enzymes that these physical factors cause?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
- Define enzyme inhibition. Explain in detail the different types of inhibitions with suitable examplesarrow_forwardConsider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.arrow_forwardEnzyme inhibition (compare and contrast reversible and irreversible inhibitors)arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License