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BCH 367 CH-7 UPDATED EXAM QUESTIONS AND CORRECT ANSWERS

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BCH 367 CH-7 UPDATED EXAM QUESTIONS AND CORRECT ANSWERS When an enzyme is operating at Vmax, the enzyme: a) displays zero-order kinetics. b) displays second-order kinetics. c) displays pseudo—first-order kinetics. d) displays kinetics dependent upon the number of reactants specific to that enzyme system. e) displays first-order kinetics. - CORRECT ANSWERS a Enzymes that follow simple Michaelis-Menten kinetics are called Michaelis-Menten enzymes. Alternatively, enzymes that regulate the flux of biochemical through metabolic pathways are called _____ enzymes. - CORRECT ANSWERS allosteric Which of the following is a CORRECT unit for a second-order rate constant? a) M/s b)M_1 c)M_1 s_1 d)M/s_1 e) M - CORRECT ANSWERS c Allosteric enzymes are _____, where _____ at one site _____. a) isozymes; the activity; is different from the activity at a different site

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BCH 367 CH-7 UPDATED EXAM QUESTIONS
AND CORRECT ANSWERS
When an enzyme is operating at Vmax, the enzyme:



a) displays zero-order kinetics.

b) displays second-order kinetics.

c) displays pseudo—first-order kinetics.

d) displays kinetics dependent upon the number of reactants specific to that enzyme system.

e) displays first-order kinetics. - CORRECT ANSWERS a



Enzymes that follow simple Michaelis-Menten kinetics are called Michaelis-Menten enzymes.
Alternatively, enzymes that regulate the flux of biochemical through metabolic pathways are
called _____ enzymes. - CORRECT ANSWERS allosteric



Which of the following is a CORRECT unit for a second-order rate constant?



a) M/s

b)M_1

c)M_1 s_1

d)M/s_1

e) M - CORRECT ANSWERS c



Allosteric enzymes are _____, where _____ at one site _____.



a) isozymes; the activity; is different from the activity at a different site

, b) isozymes; activity; affects the activity at a different site

c) cooperative; proteolytic cleavage; increases the activity of the enzyme

d) cooperative; activity; affects the activity at a different site

e) cooperative; inhibition; increases the ability of another site to bind substrate. - CORRECT
ANSWERS d



The Michaelis constant, KM:



a) is equal to ½Vmax.

b) is equal to the velocity of the reaction when the enzyme is 50% saturated with substrate.

c) is equal to the substrate concentration when the velocity of the reaction is 50% of the
maximum velocity.

d) is equal to the rate constant, k, when the reaction is in the steady state. - CORRECT
ANSWERS c



Which of the following statements about allosteric enzymes is true?



a) Allosteric enzymes follow Michaelis-Menten kinetics.

b) Allosteric enzymes can exist in an R state, which has a low affinity for substrate.

c) Allosteric enzymes have quaternary structure.

d) Allosteric enzymes capture the binding energy of the substrate to catalyze otherwise
thermodynamically unfavorable reactions. - CORRECT ANSWERS c



In a pseudo —first-order reaction:



a) a second-order reaction appears to be a first-order reaction.

b) a first-order reaction appears to be a second-order reaction.

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