Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN: 9781305389892
Author: Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher: Cengage Learning
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Chapter 6, Problem 1ITD
Summary Introduction
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The ∆G for the parent polypeptide and the mutated polypeptide binding to the protein.
Introduction:
The
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Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below.
Construct a Lineweaver-Burk plot to answer the following questions: (a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor? (b) What kind of an inhibitor is threo-sphingosine? Explain.
The nerve gas sarin acts as a poison by covalently bonding to a hydroxyl group in the active site of the enzyme acetylcholinesterase. This binding results in a higher-than-normal amount of acetylcholine at a nerve synapse, resulting in muscle spasms. From this description, would you expect sarin to be a competitive, noncompetitive, or irreversible inhibitor?
noncompetitive inhibitor
irreversible inhibitor
competitive inhibitor
You are investigating inhibitors of chymotrypsin, and the two molecules shown on the right (A&B) are being considered. Draw a Lineweaver-Burke plot showing the expected effect of each of these molecules on normal chymotrypsin kinetics. Indicate which molecule you would pick as the better inhibitor.
You want to improve the inhibitor you selected above. Briefly describe one key change you could make to your molecule to make it a better inhibitor. Justify your answer.
Chapter 6 Solutions
Biology: The Dynamic Science (MindTap Course List)
Ch. 6.1 - Prob. 1SBCh. 6.1 - In thermodynamics, what is meant by an isolated...Ch. 6.2 - Prob. 1SBCh. 6.2 - Prob. 2SBCh. 6.2 - Distinguish between exergonic and endergonic...Ch. 6.3 - Prob. 1SBCh. 6.3 - How are coupled reactions important to cell...Ch. 6.4 - How do enzymes increase the rates of the reaction...Ch. 6.4 - Can enzymes alter the G of a reaction?Ch. 6.5 - Prob. 1SB
Ch. 6.5 - What is the difference between competitive and...Ch. 6.5 - Prob. 3SBCh. 6.6 - Prob. 1SBCh. 6 - The capacity to do work best defines: a metabolic...Ch. 6 - The assembly of proteins from amino acids is best...Ch. 6 - When two glucose molecules react to form maltose:...Ch. 6 - When glucose reacts with ATP to form...Ch. 6 - In the following graph: A represents the product....Ch. 6 - Which of the following methods is not used by...Ch. 6 - In an enzymatic reaction: a. the enzyme leaves the...Ch. 6 - Which of the following statements about the...Ch. 6 - Which of the following statements about inhibition...Ch. 6 - Which of the following statements is incorrect? a....Ch. 6 - Prob. 11TYKCh. 6 - Discuss Concepts Trace the flow of energy through...Ch. 6 - Prob. 13TYKCh. 6 - Prob. 14TYKCh. 6 - Prob. 15TYKCh. 6 - Prob. 16TYKCh. 6 - Prob. 17TYKCh. 6 - Prob. 1ITDCh. 6 - Prob. 2ITDCh. 6 - Prob. 3ITD
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- Sphingosine 1-phosphate (SPP) is important for cell survival. The synthesis of SPP from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below .[Sphingosine], μM 2.5 3.5 5 10 20 50 v0(mg·minꟷ1) no inhibitor 32.3 40 50.872 87.7 115.4 v0(mg·minꟷ1)with threo-sphingosine 8.5 11.5 14.6 25.4 43.9 70.8 Construct a Lineweaver-Burk plot to answer the following questions:(A)What are the apparent KMand Vmaxvalues in the presence and absence of the inhibitor?(B)What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.arrow_forwardMany types of cells are able to use membrane-spanning transport proteins and a source of energy to drive the active transport of glucose across the cell membrane. Leť's consider a specific protein that is able to transport (from outside the cell into the cytoplasm) one molecule of glucose for each molecule of ATP the protein hydrolyzes. The details of this process are not important for this problem except that you can treat it like equilibrium process. The overall reaction and the associated AG at 298 K for this process are given below. Glc(out) + ATP + H20 = Glc(in) + ADP + P at T = 298 K, AG = -31.3 kJ mol-1 Additional Information: • P. is "inorganic phosphate" (i.e. PO4²- & related species). At equilibrium, [P] = 3 x 10-3 M. • The cell maintains a ratio of ATP to ADP of about 20 (i.e. [ATP]/[ADP] = 20). • The maximum ratio of [Glc(in)] to [Glc(out)] occurs when the system is at equilibrium. a) Write an expression for the equilibrium constant for this process. b) Your expression for…arrow_forwardThe enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidlyarrow_forward
- Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows in the picture Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland.Tartrate ion can strongly inhibit the phosphatase from the prostate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum?arrow_forwardConsider the binding reaction L + R → LR, where L is a ligand and R is its receptor. When 1 × 10−3 M of L is added to a solution containing 5 × 10−2 M of R, 90 percent of the L binds to form LR. What is the Keq of this reaction? How will the Keq be affected by the addition of a protein that facilitates (catalyzes) this binding reaction? What is the dissociation equilibrium constant Kd?arrow_forwardAcid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostrate gland. The enzyme from the prostrate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostrate gland. Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in human blood serum?arrow_forward
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