3. Ehylene glycol, the main ingredient in antifreeze, is an odorless, colorless, sweet tasting water-soluble chemical that, when ingested, is a toxic poison. The treatment for ethylene glycol poisoning involves emergency procedures that include intravenous doses of ethanol for several hours. To understand how this treatment works, you need to know that ethylene glycol is metabolized by the enzyme alcohol dehydrogenase (ADH) into four products, and these products are actual toxic agents. If this reaction can be inhibited, then the kidneys will eliminate the ethylene glycol intact before the toxins are produced. Chemist know that ADH has 100x greater affinity for ethanol than for ethylene glycol. Given your new knowledge of enzyme activity and inhibitors, speculate about the mechanism by which ethanol prevents ethylene glycol poisoning. Hint: is a non-competitive inhibitor or competitive inhibitor involved here?

3. Ehylene glycol, the main ingredient in antifreeze, is an odorless, colorless, sweet tasting water-soluble chemical that, when ingested, is a toxic poison. The treatment for ethylene glycol poisoning involves emergency procedures that include intravenous doses of ethanol for several hours. To understand how this treatment works, you need to know that ethylene glycol is metabolized by the enzyme alcohol dehydrogenase (ADH) into four products, and these products are actual toxic agents. If this reaction can be inhibited, then the kidneys will eliminate the ethylene glycol intact before the toxins are produced. Chemist know that ADH has 100x greater affinity for ethanol than for ethylene glycol. Given your new knowledge of enzyme activity and inhibitors, speculate about the mechanism by which ethanol prevents ethylene glycol poisoning. Hint: is a non-competitive inhibitor or competitive inhibitor involved here?

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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1. In Clinical Chemistry, are enzymatic methods for determining glucose, cholesterol and uric acid more preferred than non-enzymatic methods? Why or Why not?
1. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 2. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
The assembly of proteins from amino acids is best described as: a. a conversion of kinetic energy to potential energy reaction. b. an entropy reaction. c. a catabolic reaction. d. an anabolic reaction. e. an energy-free reaction.
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
When glucose reacts with ATP to form glucose-6-phosphate: a. the synthesis of glucose-6-phosphate is exergonic. b. ADP is at a higher energy level than ATP. c. glucose-6-phosphate is at a higher energy level than glucose. d. because ATP donates a phosphate to glucose, this is not a coupled reaction. e. the reaction is spontaneous.
When two glucose molecules react to form maltose: a. the reaction represents a negative G. b. free energy had to be available to allow the reaction to proceed. c. the reaction is exothermic. d. it supports the second law of thermodynamics, which states there is tendency of the universe toward disorder. e. the resulting product has less potential energy than the reactants.
Which of the following comparisons or contrasts between endergonic and exergonic reactions is false? Endergonic reactions have a positive ?G and exergonic reactions have a negative ?G Endergonic reactions consume energy and exergonic reactions release energy Both endergonic and exergonic reactions require a small amount of energy to overcome an activation barrier Endergonic reactions take place slowly and exergonic reactions take place quickly.
Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
1.A student was given two test tubes. One tube contains a reaction catalyzed by an inorganic catalyst, while the second tube contains a reaction catalyzed by an enzyme which is protein in nature. Give two laboratory procedures which you can perform to differentiate which of the two tubes contain an enzyme-catalyzed reaction. 2. List the enzymes whose levels are elevated in blood serum as a result of hepatitis or cirrhosis of the liver.
2. One manifestation of cytochrome oxidase deficiency in humans is severe muscle weakness. Briefly explain why. 3. Clostridium bacteria are killed in the presence of molecular oxygen. Would you expect Clostridium to produce catalase? Briefly explain.
1. Why is the chemical logic behind the phosphorylation of glucose by hexokinase? a. So that we end the preparatory phase with 2 3-carbon compounds. b. to provide a substrate for phosphohexose isomerase. c. "Locks" Glucose in the cell. d. to decrease the ΔG of the next reaction. 2. What type of reaction does glyceraldehyde-3-phosphate dehydrogenase catalyze? a. isomerization b. group transfer c. oxidation d. dehydration