EP FUND.OF GENERAL,ORG...-MOD.MASTERING
8th Edition
ISBN: 9780134326061
Author: McMurry
Publisher: PEARSON CO
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Textbook Question
Chapter 19, Problem 19.58AP
The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.
- (a) Describe how an enzyme inhibitor of each type works.
- (b) What kinds of bonds are formed between an enzyme and each of these three kinds of inhibitors?
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The text discusses three forms of enzyme inhibition: uncompetitive inhibition, competitive inhibition, and irreversible inhibition.(a) Describe how an enzyme inhibitor of each type works.(b) What kinds of bonds are formed between an enzymeand each of these three kinds of inhibitors?
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?
What are two major types of enzyme inhibitors? Give an example of each
Chapter 19 Solutions
EP FUND.OF GENERAL,ORG...-MOD.MASTERING
Ch. 19.1 - Prob. 19.1PCh. 19.1 - The enzyme LDH converts lactate to pyruvate. In...Ch. 19.2 - The cofactors NAD+, Cu2+, Zn2+, coenzyme A, FAD,...Ch. 19.3 - Describe the reactions that you would expect these...Ch. 19.3 - Prob. 19.5PCh. 19.3 - Prob. 19.6PCh. 19.3 - Prob. 19.7PCh. 19.3 - Prob. 19.8PCh. 19.4 - Prob. 19.9KCPCh. 19.5 - Prob. 19.10KCP
Ch. 19.5 - Prob. 19.11PCh. 19.5 - Prob. 19.12PCh. 19.6 - Prob. 19.13PCh. 19.6 - Prob. 19.14PCh. 19.7 - (a) L-Threonine is converted to L-isoleucine in a...Ch. 19.8 - AZT (zidovudine) inhibits the synthesis of the HIV...Ch. 19.8 - Prob. 19.3CIAPCh. 19.8 - Prob. 19.16PCh. 19.9 - Does the enzyme described in each of the following...Ch. 19.9 - Prob. 19.18PCh. 19.9 - Compare the structures of vitamin A and vitamin C....Ch. 19.9 - Prob. 19.20PCh. 19.9 - Prob. 19.21KCPCh. 19.9 - Prob. 19.22PCh. 19.9 - Prob. 19.4CIAPCh. 19.9 - Prob. 19.6CIAPCh. 19.9 - Prob. 19.7CIAPCh. 19.9 - Enzyme levels in blood are often elevated in...Ch. 19.9 - Prob. 19.9CIAPCh. 19.9 - Prob. 19.23PCh. 19 - Prob. 19.24UKCCh. 19 - Prob. 19.25UKCCh. 19 - Prob. 19.26UKCCh. 19 - Prob. 19.27UKCCh. 19 - Prob. 19.28APCh. 19 - Explain how the following mechanisms regulate...Ch. 19 - Prob. 19.30APCh. 19 - Prob. 19.31APCh. 19 - Prob. 19.32APCh. 19 - Prob. 19.33APCh. 19 - Prob. 19.34APCh. 19 - Prob. 19.35APCh. 19 - Prob. 19.36APCh. 19 - Prob. 19.37APCh. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - Name an enzyme that acts on each molecule. (a)...Ch. 19 - What features of enzymes make them so specific in...Ch. 19 - Describe in general terms how enzymes act as...Ch. 19 - Prob. 19.42APCh. 19 - Prob. 19.43APCh. 19 - Prob. 19.44APCh. 19 - Prob. 19.45APCh. 19 - Prob. 19.46APCh. 19 - Prob. 19.47APCh. 19 - What is the difference between the lock-and-key...Ch. 19 - Why is the induced-fit model a more likely model...Ch. 19 - Prob. 19.50APCh. 19 - Prob. 19.51APCh. 19 - How do you explain the observation that pepsin, a...Ch. 19 - Prob. 19.53APCh. 19 - Prob. 19.54APCh. 19 - Prob. 19.55APCh. 19 - Prob. 19.56APCh. 19 - Prob. 19.57APCh. 19 - The text discusses three forms of enzyme...Ch. 19 - Prob. 19.59APCh. 19 - Prob. 19.60APCh. 19 - Prob. 19.62APCh. 19 - Prob. 19.63APCh. 19 - The meat tenderizer used in cooking is primarily...Ch. 19 - Prob. 19.65APCh. 19 - Why do allosteric enzymes have two types of...Ch. 19 - Prob. 19.67APCh. 19 - Prob. 19.68APCh. 19 - Prob. 19.69APCh. 19 - Prob. 19.70APCh. 19 - Prob. 19.71APCh. 19 - Prob. 19.72APCh. 19 - Prob. 19.73APCh. 19 - Prob. 19.74APCh. 19 - Prob. 19.75APCh. 19 - Prob. 19.76APCh. 19 - Prob. 19.77APCh. 19 - Prob. 19.78APCh. 19 - Prob. 19.79APCh. 19 - Prob. 19.80CPCh. 19 - Prob. 19.81CPCh. 19 - Prob. 19.82CPCh. 19 - Prob. 19.83CPCh. 19 - Prob. 19.84CPCh. 19 - Prob. 19.85CPCh. 19 - Prob. 19.86CPCh. 19 - Prob. 19.87CPCh. 19 - Prob. 19.88GPCh. 19 - The ability to change a selected amino acid...Ch. 19 - Prob. 19.90GPCh. 19 - Prob. 19.91GP
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by noncovalent interactions? Why?arrow_forwarda) Draw one example of an interaction the enzyme could provide that would stabilize this transition state. please draw it by hand so i can understand it better. b) What is the consequence of this stabilization for the overall reaction? Briefly explain your reasoning.arrow_forwardAll 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_forward
- A) Why most therapeutic inhibitors (prescription medications) that are enzyme inhibitors function through a competitive inhibition mechanism. B) Describe a circumstance/reason that a drug company would specifically choose to develop a medication that inhibited an enzyme through a mechanism other than competitive inhibition.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_forwardA mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.arrow_forward
- 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?arrow_forwardWhat happens to a denatured enzyme regarding its functionality? How can that result be explained with the help of the lock and key model?arrow_forwardDefine enzyme inhibition. Explain in detail the different types of inhibitions with suitable examples.arrow_forward
- Drug 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_forwardFor each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result. A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glucose to fructose. This reaction is catalyzed by a(n) (dehydrogenase, isomerase, kinase, phosphatase).arrow_forwardFor each pair of biomolecules, identify the type of reaction (oxidation‑reduction, hydrolysis, isomerization, group transfer, or internal rearrangement) required to convert the first molecule to the second. In each case, indicate the general type of enzyme and cofactor(s) or reactants required, and any other products that would result. A(n) (hydrolysis, oxidation reduction, group transfer, isomerization, internal rearrangment) reaction converts glycerol to glycerol 3‑phosphate. This reaction requires (ADP and a kinase, ATP and a phosphatase, ATP and a kinase, ADP and a phosphatase).arrow_forward
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