Exam 7: Enzyme Mechanisms
Exam 1: Principles of Biochemistry98 Questions
Exam 2: Physical Biochemistry: Energy Conversion,water,and Membranes99 Questions
Exam 3: Nucleic Acid Structure and Function100 Questions
Exam 4: Protein Structure100 Questions
Exam 5: Methods in Protein Biochemistry98 Questions
Exam 6: Protein Function113 Questions
Exam 7: Enzyme Mechanisms105 Questions
Exam 8: Cell Signaling Systems102 Questions
Exam 9: Glycolysis: a Paradigm of Metabolic Regulation100 Questions
Exam 10: The Citrate Cycle100 Questions
Exam 11: Oxidative Phosphorylation98 Questions
Exam 12: Photosynthesis100 Questions
Exam 13: Carbohydrate Structure and Function100 Questions
Exam 14: Carbohydrate Metabolism100 Questions
Exam 15: Lipid Structure and Function98 Questions
Exam 16: Lipid Metabolism100 Questions
Exam 17: Amino Acid Metabolism100 Questions
Exam 18: Nucleotide Metabolism98 Questions
Exam 19: Metabolic Integration101 Questions
Exam 20: Dna Replication, repair, and Recombination99 Questions
Exam 21: Rna Synthesis, processing, and Gene Silencing100 Questions
Exam 22: Protein Synthesis, posttranslational Modification, and Transport100 Questions
Exam 23: Gene Regulation99 Questions
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What is the appropriate order of the following steps?
A.Glutamine binding to uridylyltransferase
B.Adenylation of glutamine synthetase
C.Deuridylation of glutamine synthetase adenylyltransferase
(Multiple Choice)
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If the rate constant for a reaction is determined to be equal to v / [Q][R],the reaction is the conversion of
(Multiple Choice)
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In the formation of an ESI complex,__________ inhibition can result.
(Multiple Choice)
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An enzyme is crystallized in preparation for X-ray crystallography.The crystal is then soaked in a solution of substrate and the crystal shatters.Propose a reason for this result.
(Essay)
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Hexokinase catalyzes the first step of glycolysis,which occurs in the cell cytoplasm.The protocol for an in vitro enzyme activity assay of hexokinase suggests that the assay is carried out at a pH of 7.4.Predict what may occur if the assay is carried out at a pH of 8.8 instead.Explain your reasoning.
(Essay)
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A kinase adds a phosphate group to a target enzyme,altering the catalytic efficiency of the enzyme.This is an example of
(Multiple Choice)
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Using words,define initial velocity (v0)for an enzyme-catalyzed reaction.
(Essay)
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Enzymes usually bind substrates with __________ affinity and __________ specificity.
(Multiple Choice)
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Complete the following statement: The NH groups of Ser195 and Gly193 in chymotrypsin are able to stabilize the intermediate of the reaction by
(Short Answer)
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If an enzyme carries out acid-base catalysis,which of the following amino acids could act as general acid?
(Multiple Choice)
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The side chains of the amino acids that make up the catalytic triad of chymotrypsin contain all EXCEPT
(Multiple Choice)
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Which type of reaction does not change the molecular formula of the product compared with that of the substrate?
(Multiple Choice)
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A mutation results in the change of Ser to Asp in the substrate binding pocket of chymotrypsin.Most likely,the mutant enzyme will
(Multiple Choice)
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Acetylcholinesterase is an important enzyme in the nervous system.Acetylcholinesterase activity is blocked by the nerve agent sarin gas,which forms a covalent bond with a Ser in the active site of the enzyme.Sarin gas is a(n)
(Multiple Choice)
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Which pair correctly matches the coenzymes most often used to mediate the described redox reactions?
(Multiple Choice)
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Nitrite reductase contains two histidine amino acids that coordinate a Cu2+ ion.When the ion is present in the enzyme,the ion is a __________ and the enzyme is a __________.
(Multiple Choice)
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Which of the following is true of a coenzyme but NOT true of a prosthetic group?
(Multiple Choice)
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An enzyme can increase the rate of a reaction inside a cell by __________ the energy of the __________.
(Multiple Choice)
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