Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 6, Problem 47RE
RECALL How can competitive and pure noncompetitive inhibition be distinguished in terms of
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Chapter 6 Solutions
Biochemistry
Ch. 6 - RECALL How does the catalytic effectiveness of...Ch. 6 - RECALL Are all enzymes proteins?Ch. 6 - MATHEMATICAL Catalase breaks down hydrogen...Ch. 6 - REFLECT AND APPLY Give two reasons why enzyme...Ch. 6 - RECALL For the reaction of glucose with oxygen to...Ch. 6 - REFLECT AND APPLY Would nature rely on the same...Ch. 6 - REFLECT AND APPLY Suggest a reason why heating a...Ch. 6 - REFLECT AND APPLY A model is proposed to explain...Ch. 6 - REFLECT AND APPLY Does the presence of a catalyst...Ch. 6 - REFLECT AND APPLY What effect does a catalyst have...
Ch. 6 - REFLECT AND APPLY An enzyme catalyzes the...Ch. 6 - REFLECT AND APPLY Can the presence of a catalyst...Ch. 6 - RECALL For the hypothetical reaction 3A+2B2C+3D...Ch. 6 - REFLECT AND APPLY The enzyme lactate dehydrogenase...Ch. 6 - REFLECT AND APPLY Would you use a pH meter to...Ch. 6 - REFLECT AND APPLY Suggest a reason for carrying...Ch. 6 - RECALL Distinguish between the lock-and-key and...Ch. 6 - RECALL Using an energy diagram, show why the...Ch. 6 - REFLECT AND APPLY Other things being equal, what...Ch. 6 - REFLECT AND APPLY Amino acids that are far apart...Ch. 6 - REFLECT AND APPLY If only a few of the amino acid...Ch. 6 - RECALL Show graphically how the reaction velocity...Ch. 6 - RECALL Define steady state, and comment on the...Ch. 6 - RECALL How is the turnover number of an enzyme...Ch. 6 - MATHEMATICAL For an enzyme that displays...Ch. 6 - MATHEMATICAL Determine the values of KM and Vmax...Ch. 6 - MATHEMATICAL The kinetic data in the following...Ch. 6 - MATHEMATICAL The enzyme -methylaspartase catalyzes...Ch. 6 - MATHEMATICAL The hydrolysis of a...Ch. 6 - MATHEMATICAL For the Vmax obtained in Question 26,...Ch. 6 - MATHEMATICAL You do an enzyme kinetic experiment...Ch. 6 - REFLECT AND APPLY The enzyme D-amino acid oxidase...Ch. 6 - REFLECT AND APPLY Why is it useful to plot rate...Ch. 6 - REFLECT AND APPLY Under what conditions can we...Ch. 6 - BIOCHEMICAL CONNECTIONS Why does acetazolamide...Ch. 6 - BIOCHEMICAL CONNECTIONS How did scientists...Ch. 6 - BIOCHEMICAL CONNECTIONS How do the KM values for...Ch. 6 - Prob. 38RECh. 6 - RECALL What are the three most common mechanisms...Ch. 6 - RECALL What is the biggest difference between a...Ch. 6 - RECALL How do scientists determine the KM of a...Ch. 6 - Prob. 42RECh. 6 - Prob. 43RECh. 6 - RECALL Do all enzymes display kinetics that obey...Ch. 6 - RECALL How can you recognize an enzyme that does...Ch. 6 - RECALL If we describe an enzyme like aspartate...Ch. 6 - RECALL How can competitive and pure noncompetitive...Ch. 6 - RECALL Why does a competitive inhibitor not change...Ch. 6 - RECALL Why does a pure noncompetitive inhibitor...Ch. 6 - RECALL Distinguish between the molecular...Ch. 6 - RECALL Can enzyme inhibition be reversed in all...Ch. 6 - RECALL Why is a Lineweaver-Burk plot useful in...Ch. 6 - RECALL Where do lines intersect on a...Ch. 6 - RECALL What is the difference between pure and...Ch. 6 - REFLECT AND APPLY Why can we say that having a...Ch. 6 - REFLECT AND APPLY When we compare the binding of I...Ch. 6 - RECALL Why does the apparent KM decrease in the...Ch. 6 - RECALL What is a suicide substrate? Why are they...Ch. 6 - RECALL If we made a Lineweaver-Burk plot of an...Ch. 6 - Prob. 60RECh. 6 - MATHEMATICAL For the following aspartase reaction...Ch. 6 - REFLECT AND APPLY Is it good (or bad) that enzymes...Ch. 6 - REFLECT AND APPLY Noncompetitive inhibition is a...Ch. 6 - BIOCHEMICAL CONNECTIONS You have been hired by a...Ch. 6 - REFLECT AND APPLY Would you expect an irreversible...Ch. 6 - REFLECT AND APPLY Would you expect the structure...Ch. 6 - Prob. 67RECh. 6 - Prob. 68RE
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- RECALL Where do lines intersect on a Lineweaver-Burk plot showing competitive inhibition? On a Lineweaver-Burk plot showing noncompetitive inhibition?arrow_forwardREFLECT AND APPLY Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?arrow_forwardREFLECT AND APPLY Noncompetitive inhibition is a limiting case in which the effect of binding inhibitor has no effect on the affinity for the substrate and vice versa. Suggest what a LineweaverBurk plot would look like for an inhibitor that had a reaction scheme similar to that on page 159 (noncompetitive inhibition reaction), but where binding inhibitor lowered the affinity of EI for the substrate.arrow_forward
- REFLECT AND APPLY Is amino acid activation energetically favored? Why or why not?arrow_forwardREFLECT AND APPLY Would nature rely on the same enzyme to catalyze a reaction either way (forward or backward) if the DG were 0.8kcalmol1? If it were 5.3kcalmol1?arrow_forwardREFLECT AND APPLY Consider the structures of arabinose and ribose. Explain why nucleotide derivatives of arabinose, such as ara-C and ara-A, are effective metabolic poisons.arrow_forward
- RECALL Show graphically how the reaction velocity depends on the enzyme concentration. Can a reaction be saturated with enzyme?arrow_forwardREFLECT AND APPLY When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?arrow_forwardREFLECT AND APPLY Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by non-covalent interactions? Why?arrow_forward
- REFLECT AND APPLY Sulfanilamide and related sulfa drugs were widely used to treat diseases of bacterial origin before penicillin and more advanced drugs were readily available. The inhibitory effect of sulfanilamide on bacterial growth can be reversed by p-aminobenzoate. Suggest a mode of action for sulfanilamide.arrow_forwardREFLECT AND APPLY Why is it somewhat misleading to study bio- chemical pathways separately?arrow_forwardREFLECT AND APPLY Suggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is the decrease of activity frequently much less when the solution contains high concentrations of the substrate?arrow_forward
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