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Hexokinase catalyzes the phosphorylation of glucose to glucose 6-phosphate. Hexokinase belongs to which enzyme class?


A) transferase
B) ligase
C) oxidoreductase
D) hydrolase

E) All of the above
F) A) and C)

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Define the term zymogen.

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Zymogen is the inactive precur...

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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 _.


A) cofactor; apoenzyme
B) cofactor; holoenzyme
C) coenzyme; apoenzyme
D) coenzyme; holoenzyme

E) A) and B)
F) A) and C)

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The catalytic triad of chymotrypsin is composed of His57, Ser195, and


A) Gly193.
B) Glu103.
C) Asp120.
D) Asp102.

E) B) and C)
F) None of the above

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An enzyme undergoes a mutation that causes it to lose the ability to be regulated via phosphorylation. Which of the following mutations may lead to this loss of regulation? Assume that the overall structure is not altered by the mutation.


A) Ser \rightarrow Thr
B) Thr \rightarrow Ser
C) Tyr \rightarrow Phe
D) Ser \rightarrow Tyr

E) None of the above
F) B) and C)

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Which of the following is true of the induced-fit model of enzyme catalysis but NOT of the lock and key model of enzyme catalysis?


A) It was proposed by Emil Fischer.
B) It involves weak interactions of a substrate with an enzyme.
C) It involves a conformational change of the enzyme.
D) It involves noncovalent interactions of the substrate with the enzyme.

E) B) and C)
F) C) and D)

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Propose an experiment to determine the presence of a predicted hydrophobic channel in a newly discovered enzyme. At your disposal you have the purified enzyme, the ability to analyze the enzyme by X-ray crystallography, a spectrophotometer, the enzyme substrate, and polyethylene glycol. Be sure to explain how the results will determine if the protein contains a hydrophobic channel.

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To determine the presence of a predicted...

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Phosphorylation of __________ in glycogen phosphorylase shifts the enzyme to the __________.


A) Tyr397; T state
B) Tyr397; R state
C) Ser14; T state
D) Ser14; R state

E) None of the above
F) C) and D)

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Using words, define initial velocity (v0) for an enzyme-catalyzed reaction.

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Initial velocity (v0) for an e...

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Refer to the reaction coordinate diagram below. At what point is there a maximum number of interactions between the enzyme and the compound that it is binding? Refer to the reaction coordinate diagram below. At what point is there a maximum number of interactions between the enzyme and the compound that it is binding?   A)  A B)  B C)  C D)  D


A) A
B) B
C) C
D) D

E) A) and C)
F) All of the above

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The regulation of a biomolecule through the addition or removal of a molecular tag involves __________ reactions.


A) coenzyme-dependent redox
B) reversible covalent modification
C) metabolite transformation
D) isomerization

E) B) and D)
F) C) and D)

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Justify how an enzyme that catalyzes a hydrolysis reaction does not contradict the concept that enzyme active sites are microenvironments that exclude excess water.

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An enzyme that catalyzes a hydrolysis re...

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An experiment is performed in which the kinetics of an enzyme-catalyzed reaction at different pHs is monitored. It is found that the Km does not change but that the kcat increases as the pH goes above 7. Which of the following is true?


A) A chemical group within the enzyme that has a pKa of around 7 is likely involved in the catalytic mechanism.
B) A chemical group with a pKa of around 7 must be deprotonated in order for substrate to bind.
C) A chemical group with a pKa of around 7 must be positively charged in order for the substrate to bind.
D) Protons are acting as positive heterotropic allosteric effectors of this enzyme.

E) A) and B)
F) A) and C)

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KM is equal to


A) "k1 / (k - 1 + k2) ."
B) "(k - 1 + k2) / k1."
C) "12 vmax."
D) "vmax[S] / v0."

E) None of the above
F) All of the above

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The conversion of 2-phosphoglycerate to phosphoenolpyruvate is an example of which type of reaction?


A) hydrolysis
B) dehydration
C) isomerization
D) condensation

E) A) and B)
F) A) and C)

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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


A) covalent modification.
B) proteolytic processing.
C) binding of regulatory molecules.
D) feedback inhibition.

E) C) and D)
F) A) and C)

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A Lineweaver-Burk plot displays parallel lines for an enzyme in the absence and presence of increasing amounts of an inhibitor. The inhibitor in this experiment


A) binds both the free enzyme and the ES complex.
B) is competitive.
C) alters the Km but not the vmax.
D) is uncompetitive.

E) A) and B)
F) C) and D)

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The Lineweaver-Burk plot shows data obtained for an enzyme in the absence and presence of a reversible inhibitor. Which type of inhibitor was used in the experiment? The Lineweaver-Burk plot shows data obtained for an enzyme in the absence and presence of a reversible inhibitor. Which type of inhibitor was used in the experiment?   A)  competitive B)  uncompetitive C)  mixed D)  noncompetitive


A) competitive
B) uncompetitive
C) mixed
D) noncompetitive

E) B) and D)
F) All of the above

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What three amino acids are targeted for phosphorylation by kinases?

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Serine, th...

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A patient presents with symptoms associated with the disease beriberi. An analysis of pyruvate dehydrogenase complex activity shows significantly reduced levels from normal. Predict how a deficiency in a coenzyme may be the culprit. Specify the coenzyme involved.

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Beriberi disease is caused by reduced py...

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