Exam 6: Mechanisms of Enzymes
Exam 1: Introduction to Biochemistry60 Questions
Exam 2: Water80 Questions
Exam 3: Amino Acids and the Primary Structures of Proteins85 Questions
Exam 4: Proteins: Three-Dimensional Structure and Function101 Questions
Exam 5: Properties of Enzymes80 Questions
Exam 6: Mechanisms of Enzymes75 Questions
Exam 7: Coenzymes and Vitamins80 Questions
Exam 8: Carbohydrates77 Questions
Exam 9: Lipids and Membranes85 Questions
Exam 10: Introduction to Metabolism75 Questions
Exam 11: Glycolysis74 Questions
Exam 12: Gluconeogenesis, the Pentose Phosphate Pathway, and Glycogen Metabolism75 Questions
Exam 13: The Citric Acid Cycle75 Questions
Exam 14: Electron Transport and Oxidative Phosphorylation82 Questions
Exam 15: Photosynthesis70 Questions
Exam 16: Lipid Metabolism75 Questions
Exam 17: Amino Acid Metabolism73 Questions
Exam 18: Nucleotide Metabolism65 Questions
Exam 19: Nucleic Acids83 Questions
Exam 20: Dna Replication, Repair, and Recombination76 Questions
Exam 21: Transcription and Rna Processing75 Questions
Exam 22: Protein Synthesis85 Questions
Exam 23: Recombinant Dna Technology73 Questions
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The reaction catalyzed by a certain phosphatase enzyme is found to follow ping-pong kinetics and involves the transfer of a phosphate group from substrate A to substrate B. Which mode of catalysis is likely for this reaction?
(Multiple Choice)
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Active trypsin formation by the action of enteropeptidase can be viewed as the master activation step because
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Zymogens are inactive enzyme precursors which are made active by
(Multiple Choice)
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A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction?
(Multiple Choice)
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A key role of the hydroxyl group at position 6 in the purine ring in the formation of a transition state by the enzyme adenosine deaminase is obtained by comparing a and a .
(Multiple Choice)
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Antibodies raised against transition state analogs are always enzymatic.
(True/False)
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An enzymeʹs active site contains an arginine residue and a glutamate residue with pKaʹs of 2.9 and 9.1, respectively. Both residues are actively involved in the catalytic mechanism and they are the only two ionizable residues in the active site. What would you expect for the optimum pH of the enzyme?
(Multiple Choice)
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The movement of is key to understanding chemical and enzymatic reactions.
(Multiple Choice)
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On the energy diagram below, which point represents an intermediate? 
(Multiple Choice)
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Which amino acid is least likely to participate in acid-base catalysis?
(Multiple Choice)
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Glycoside hydrolases such as bacterial cellulase have been shown to differ in mechanisms from that of lysozyme. They
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Acid-base catalysis is estimated to accelerate a typical enzymatic reaction by what factor?
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Superoxide dismutase enzyme catalysis is faster than the rate of diffusion because it
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The active site of a certain enzyme contains a serine residue. When the enzyme is incubated for a short time with its substrate, a form of the enzyme in which the active site serine is acetylated can be isolated and purified. In the native protein the serine is never found to be acetylated. This information supports .
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When the concentration of a substrate inside a cell falls below the substrate concentration at half maximal velocity .
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Which modes) of catalysis is/are classified as chemical effects? 1. Transition state stabilization
2. Acid-base catalysis
3. Covalent catalysis
4. Proximity effect
(Multiple Choice)
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Zymogens are often active only in the environment in which they are functional.
(True/False)
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Intermediates are more stable and have longer lifetimes than transition states.
(True/False)
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