30. An enzyme was obtained in Dr. Cai's lab. To study the kinetics of this enzyme, a graduate student measured the velocity of the reaction at a substrate concentration of 0.1 mM substrate. He found that after a competitive inhibitor was added, the initial rate decreased to 1/3 of the original rate. KM, the Michaelis constant, is 0.2 mm. K₁, the dissociation constant for the inhibitor binding to the enzyme, is 1.5 mM. What is the concentration of inhibitor that was added. (Hint: in the presence of the Vmax [S] competitive inhibitor, Vo ) A. 3.0 mM B. 4.5 mM C. 6.0 mM D. 7.5 mM E. 10 mM +) KM (S) (1+

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30. An enzyme was obtained in Dr. Cai's lab. To study the kinetics of this enzyme, a
graduate student measured the velocity of the reaction at a substrate concentration
of 0.1 mM substrate. He found that after a competitive inhibitor was added, the initial
rate decreased to 1/3 of the original rate. KM, the Michaelis constant, is 0.2 mm. K₁,
the dissociation constant for the inhibitor binding to the enzyme, is 1.5 mM. What is
the concentration of inhibitor that was added. (Hint: in the presence of the
Vmax [S]
competitive inhibitor, Vo
)
(1+ KM (S)
A. 3.0 mM
B. 4.5 mM
C. 6.0 mM
D. 7.5mM
E. 10 mM
Transcribed Image Text:30. An enzyme was obtained in Dr. Cai's lab. To study the kinetics of this enzyme, a graduate student measured the velocity of the reaction at a substrate concentration of 0.1 mM substrate. He found that after a competitive inhibitor was added, the initial rate decreased to 1/3 of the original rate. KM, the Michaelis constant, is 0.2 mm. K₁, the dissociation constant for the inhibitor binding to the enzyme, is 1.5 mM. What is the concentration of inhibitor that was added. (Hint: in the presence of the Vmax [S] competitive inhibitor, Vo ) (1+ KM (S) A. 3.0 mM B. 4.5 mM C. 6.0 mM D. 7.5mM E. 10 mM
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