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 46RE
RECALL If we describe an enzyme like aspartate transcarbamoylase and say that it exhibits cooperativity, what do we mean?
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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 If we made a Lineweaver-Burk plot of an irreversible inhibitor, which type of reversible inhibition would it be most likely to resemble?arrow_forwardREFLECT AND APPLY You are in the process of determining the amino acid sequence of a protein and must reconcile contradictory results. In one trial, you determine a sequence with glycine as the N-terminal amino acid and asparagine as the C-terminal amino acid. In another trial, your results indicate phenylalanine as the N-terminal amino acid and alanine as the C-terminal amino acid. How do you reconcile this apparent contradiction?arrow_forwardREFLECT AND APPLY Explain how glycogen phosphorylase is controlled allosterically and by covalent modification.arrow_forward
- REFLECT AND APPLY Is amino acid activation energetically favored? Why or why not?arrow_forwardRECALL Show graphically how the reaction velocity depends on the enzyme concentration. Can a reaction be saturated with enzyme?arrow_forwardRECALL Distinguish between the lock-and-key and induced-fit models for binding of a substrate to an enzyme.arrow_forward
- REFLECT AND APPLY A mutation that changes an alanine residue in a protein to an isoleucine leads to a loss of activity. Activity is regained when a further mutation at the same site changes the isoleucine to a glycine. Why?arrow_forwardRECALL Do all enzymes display kinetics that obey the Michaelis-Menten equation? Which ones do not?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 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_forwardRECALL Define the term reducing sugar.arrow_forwardRECALL Where do lines intersect on a Lineweaver-Burk plot showing competitive inhibition? On a Lineweaver-Burk plot showing noncompetitive inhibition?arrow_forward
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