A Pri Ter Acc 1 7°C Partly sunny Enzymes represent an important target for the development of therapeutic drugs to inhibit their activity. What could be one advantage of a pure non-competitive inhibitor as a drug compound compared to a competitive inhibitor? A A pure non-competitive inhibitor alters enzyme activity independently of substrate concentration B A pure non-competitive inhibitor will decrease the KM of the enzyme for the substrate A pure non-competitive inhibitor will occupy the substrate binding site A pure non-competitive inhibitor cannot result in any adverse side-effects Last saved 09:42:22 Questions Filter (16) ▼ Q Search K First Previous Next > Last > hp Continue O myhp

A Pri Ter Acc 1 7°C Partly sunny Enzymes represent an important target for the development of therapeutic drugs to inhibit their activity. What could be one advantage of a pure non-competitive inhibitor as a drug compound compared to a competitive inhibitor? A A pure non-competitive inhibitor alters enzyme activity independently of substrate concentration B A pure non-competitive inhibitor will decrease the KM of the enzyme for the substrate A pure non-competitive inhibitor will occupy the substrate binding site A pure non-competitive inhibitor cannot result in any adverse side-effects Last saved 09:42:22 Questions Filter (16) ▼ Q Search K First Previous Next > Last > hp Continue O myhp

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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An allosteric inhibitor does which of the following? Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding Binds to the active site and blocks it from binding substrate Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate Binds directly to the active site and mimics the substrate.
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 analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
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
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.
What is the effect of an inhibitor binding an enzyme? The enzyme is degraded. The enzyme is activated. The enzyme is inactivated. The complex is transported out of the cell
Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
Which of the following is not true about enzymes They increase ?G of reactions They are usually made of amino acids They lower the activation energy of chemical reactions Each one is specific to the particular substrate(s) to which it hinds.
Match each tern with its most suitable description. _____ reactant a. assists enzymes _____ phagocytosis b. forms at reactions end _____ lipid bilayer c. enters a reaction _____ cyclic pathway d. enzyme action _____ product e. one cell engulfs another _____ cofactor f. electron exchange _____ passive transport g. no energy input required _____ catalysis h. phospholipids + water _____ redox reaction i. goes in circles _____ first law of thermodynamics j. basis of diffusion _____ concentrarion gradient k. energy cannot be created or destroyed