Which of the following statements about transition state analog inhibitors are true? MARK ALL THAT APPLY. Group of answer choices Provide insight into catalytic mechanisms. Very potent and specific inhibitors. They have difficulty binding to the active site because they resemble the energetically unstable transition state of the substrate. Can be used as immunogens to generate catalytic antibodies.

Which of the following statements about transition state analog inhibitors are true? MARK ALL THAT APPLY. Group of answer choices Provide insight into catalytic mechanisms. Very potent and specific inhibitors. They have difficulty binding to the active site because they resemble the energetically unstable transition state of the substrate. Can be used as immunogens to generate catalytic antibodies.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.
What enzyme kinetic parameters are apparantly impacted by uncompetitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
Briefly describe 3 general catalytic mechanisms
1. There are two major categories of enzyme, inhibition, name, and describe them. 1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.
1. Explain chemotherapy in terms of specific inhibition 2. Explain why enzyme activity declines at (a)high temperature and (b) presence of heavy metal ions.
Item 35 Organic cofactors are referred to as _________. Fill in the blank Item36 Item Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e. substrate, and its effectiveness depends on product concentration. Item37 Item 37 A substance that binds to the active site of an enzyme and turns it off is called a _________ inhibitor. Fill in the blank Item 38 Lactase is an enzyme that digests lactose. True or False Item 39 Exergonic reactions do not require activation energy. True or False
1 the concentration of the enzyme competition inhibitor was 1×10-3M. If 1 µmol of the inhibitor is present inthe 1 mL reaction mixture, Indicate how much the initial degree of hydrolysis decreases as a proportion(in thepresence of inhibitors/in the absence of inhibitors) with respect to the absence of inhibitors.
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
Match each inhibitor with its effect on Michaelis-Menten reactions. Group of answer choices Vmax and apparent Vmax are equal and the apparent Km is greater than Km. The apparent Vmax is less than Vmax and the apparent Km and Km are equal The apparent Vmax and the apparent Km are both lowered to the same degree. The apparent Vmax is less than Vmax and the apparent Km can be either greater than or less than Km.
Item 35 Organic cofactors are referred to as _________. Fill in the blank 36 Item 36 Noncompetitive inhibition of an enzyme occurs when the inhibitor binds to the Multiple Choice a. allosteric site, and its effectiveness is not influenced by substrate concentration. b. allosteric site, and its effectiveness depends on substrate concentration. c. active site, and its effectiveness is not influenced by substrate concentration. d. active site, and its effectiveness depends on substrate concentration. e.substrate, and its effectiveness depends on product concentration.
An inhibitor "I" is added to the enzymatic reaction at a concentration of 1.0 g/L. The data obtained are shown in the table below. No Inhibitor With Inhibitor [S](g/L) v ([E0] = 0,015 g/L) (g/L.min) v ([E0] = 0,015 g/L)(g/L.min) 40 2,28 1,818 20 1,74 1,316 13,4 1,4 0,986 10 1,18 0,76 8 1 0,62 (a)What kind of inhibition occurred?(b)Determine Ki (in g/L) for the inhibition of the previous exercise.
Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu