A) transferase
B) ligase
C) oxidoreductase
D) hydrolase
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Multiple Choice
A) cofactor; apoenzyme
B) cofactor; holoenzyme
C) coenzyme; apoenzyme
D) coenzyme; holoenzyme
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Multiple Choice
A) Gly193.
B) Glu103.
C) Asp120.
D) Asp102.
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Multiple Choice
A) Ser Thr
B) Thr Ser
C) Tyr Phe
D) Ser Tyr
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Multiple Choice
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.
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A) Tyr397; T state
B) Tyr397; R state
C) Ser14; T state
D) Ser14; R state
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A) A
B) B
C) C
D) D
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A) coenzyme-dependent redox
B) reversible covalent modification
C) metabolite transformation
D) isomerization
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Multiple Choice
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.
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Multiple Choice
A) "k1 / (k - 1 + k2) ."
B) "(k - 1 + k2) / k1."
C) "1⁄2 vmax."
D) "vmax[S] / v0."
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Multiple Choice
A) hydrolysis
B) dehydration
C) isomerization
D) condensation
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Multiple Choice
A) covalent modification.
B) proteolytic processing.
C) binding of regulatory molecules.
D) feedback inhibition.
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Multiple Choice
A) binds both the free enzyme and the ES complex.
B) is competitive.
C) alters the Km but not the vmax.
D) is uncompetitive.
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Multiple Choice
A) competitive
B) uncompetitive
C) mixed
D) noncompetitive
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