Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Textbook Question
Chapter 7, Problem 54RE
REFLECT AND APPLY What is the relationship between a transition-state analog and the induced-fit model of enzyme kinetics?
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Chapter 7 Solutions
Biochemistry
Ch. 7 - RECALL What features distinguish enzymes that...Ch. 7 - RECALL What is the metabolic role of aspartate...Ch. 7 - RECALL What molecule acts as a positive effector...Ch. 7 - RECALL Is the term KM used with allosteric...Ch. 7 - Prob. 5RECh. 7 - Prob. 6RECh. 7 - RECALL What is a homotropic effect? What is a...Ch. 7 - RECALL What is the structure of ATCase?Ch. 7 - RECALL How is the cooperative behavior of...Ch. 7 - RECALL Does the behavior of allosteric enzymes...
Ch. 7 - RECALL Does the behavior of allosteric enzymes...Ch. 7 - RECALL Explain what is meant by K0.5.Ch. 7 - REFLECT AND APPLY Explain the experiment used to...Ch. 7 - RECALL Distinguish between the concerted and...Ch. 7 - RECALL Which allosteric model can explain negative...Ch. 7 - RECALL With the concerted model, what conditions...Ch. 7 - Prob. 17RECh. 7 - Prob. 18RECh. 7 - Prob. 19RECh. 7 - Prob. 20RECh. 7 - Prob. 21RECh. 7 - BIOCHEMICAL CONNECTIONS How does Valium work?Ch. 7 - Prob. 23RECh. 7 - Prob. 24RECh. 7 - RECALL What is the function of a protein kinase?Ch. 7 - RECALL What amino acids are often phosphorylated...Ch. 7 - REFLECT AND APPLY What are some possible...Ch. 7 - REFLECT AND APPLY Explain how phosphorylation is...Ch. 7 - REFLECT AND APPLY Explain how glycogen...Ch. 7 - Prob. 30RECh. 7 - Prob. 31RECh. 7 - RECALL Name three proteins that are subject to the...Ch. 7 - Prob. 33RECh. 7 - RECALL What are caspases?Ch. 7 - REFLECT AND APPLY Explain why cleavage of the bond...Ch. 7 - REFLECT AND APPLY Why is it necessary or...Ch. 7 - Prob. 37RECh. 7 - Prob. 38RECh. 7 - Prob. 39RECh. 7 - RECALL What are the two essential amino acids in...Ch. 7 - RECALL Why does the enzyme reaction for...Ch. 7 - REFLECT AND APPLY Briefly describe the role of...Ch. 7 - REFLECT AND APPLY Explain the function of...Ch. 7 - REFLECT AND APPLY Explain why the second phase of...Ch. 7 - Prob. 45RECh. 7 - REFLECT AND APPLY An inhibitor that specifically...Ch. 7 - REFLECT AND APPLY What properties of metal ions...Ch. 7 - RECALL In biochemistry mechanisms, what group is...Ch. 7 - Prob. 49RECh. 7 - REFLECT AND APPLY Explain the difference between...Ch. 7 - Prob. 51RECh. 7 - Prob. 52RECh. 7 - Prob. 53RECh. 7 - REFLECT AND APPLY What is the relationship between...Ch. 7 - Prob. 55RECh. 7 - BIOCHEMICAL CONNECTIONS Why can cocaine addiction...Ch. 7 - Prob. 57RECh. 7 - Prob. 58RECh. 7 - RECALL How are coenzymes related to vitamins?Ch. 7 - RECALL What type of reaction uses vitamin B6?Ch. 7 - Prob. 61RECh. 7 - Prob. 62RECh. 7 - Prob. 63RECh. 7 - BIOCHEMICAL CONNECTIONS What are some of the ways...Ch. 7 - Prob. 65RECh. 7 - Prob. 66RECh. 7 - Prob. 67RECh. 7 - Prob. 68RECh. 7 - Prob. 69RECh. 7 - Prob. 70RECh. 7 - Prob. 71RECh. 7 - Prob. 72RECh. 7 - Prob. 73RE
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- REFLECT 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 Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by non-covalent interactions? Why?arrow_forwardREFLECT AND APPLY A model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?arrow_forward
- REFLECT AND APPLY Why can we say that having a pure non- competitive inhibitor present is similar to just having less enzyme present?arrow_forwardREFLECT AND APPLY Comment on the energetics of protein folding in light of the information in this chapter.arrow_forwardREFLECT AND APPLY Other things being equal, what is a potential disadvantage of an enzyme having a very high affinity for its substrate?arrow_forward
- REFLECT 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 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_forwardREFLECT AND APPLY Why is it useful to plot rate data for enzymatic reactions as a straight line rather than as a curve?arrow_forward
- REFLECT AND APPLY Amino acids that are far apart in the amino acid sequence of an enzyme can be essential for its catalytic activity. What does this suggest about its active site?arrow_forwardREFLECT AND APPLY The enzyme D-amino acid oxidase has a very high turnover number because the D-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to 2 mM for the aromatic amino acids and in the range of 15 to 20 mM for such amino acids as serine, alanine, and the acidic amino acids. Which of these amino acids are the preferred substrates for the enzyme?arrow_forwardREFLECT AND APPLY Why is the development of catalysis important to the development of life?arrow_forward
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