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Below is the set of kinetics data of a velocity of an enzymatic reaction without inhibitor (Vo) and with an inhibitor (Voi): Which one is correct about the inhibition? Vo Voi 1 0.286 0.133 0.5 0.22 0.08 0.33 0.18 0.057 0.25 0.15 0.044 0.2 0.13 0.036 O Inhibitor decreases Vmax of the enzyme O Inhibitor is most likely structurally similar to a substrate O Inhibition of the enzyme is irreversible O Inhibitor can only bind to ES complex You are studying the kinetics of an unknown enzyme. Concentration of the enzyme is 5 micromolar. You obtained the following kinetic data: IS[ (mM) Vo, mM/s 10.83 18.57 0.02 0.04 0.07 26.76 0.1 0.15 32.50 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 What is the Km of the enzyme? O 0.1 mM 10 mM 65 mM 60 mM Which statement about the enzyme from previous question is correct? (Kinetic data are provided again just in case) IS] (mM) 0.02 Vo, mM/s 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 48.75 54.17 0.3 0.5 0.7 56.88 O Enzyme functions near catalytic perfection O Only a minor fraction of encounters between enzyme and substrate results in a reaction O Enzyme has no upper limit of catalytic efficiency O Enzyme velocity is faster than allowed by diffusion

Below is the set of kinetics data of a velocity of an enzymatic reaction without inhibitor (Vo) and with an inhibitor (Voi): Which one is correct about the inhibition? Vo Voi 1 0.286 0.133 0.5 0.22 0.08 0.33 0.18 0.057 0.25 0.15 0.044 0.2 0.13 0.036 O Inhibitor decreases Vmax of the enzyme O Inhibitor is most likely structurally similar to a substrate O Inhibition of the enzyme is irreversible O Inhibitor can only bind to ES complex You are studying the kinetics of an unknown enzyme. Concentration of the enzyme is 5 micromolar. You obtained the following kinetic data: IS[ (mM) Vo, mM/s 10.83 18.57 0.02 0.04 0.07 26.76 0.1 0.15 32.50 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 What is the Km of the enzyme? O 0.1 mM 10 mM 65 mM 60 mM Which statement about the enzyme from previous question is correct? (Kinetic data are provided again just in case) IS] (mM) 0.02 Vo, mM/s 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 48.75 54.17 0.3 0.5 0.7 56.88 O Enzyme functions near catalytic perfection O Only a minor fraction of encounters between enzyme and substrate results in a reaction O Enzyme has no upper limit of catalytic efficiency O Enzyme velocity is faster than allowed by diffusion

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Below is the set of kinetics data of a velocity of an enzymatic reaction without inhibitor (Vo) and with an inhibitor (Voi): Which one is correct about the inhibition? Vo Voi 1 0.286 0.133 0.5 0.22 0.08 0.33 0.18 0.057 0.25 0.15 0.044 0.2 0.13 0.036 O Inhibitor decreases Vmax of the enzyme O Inhibitor is most likely structurally similar to a substrate O Inhibition of the enzyme is irreversible O Inhibitor can only bind to ES complex You are studying the kinetics of an unknown enzyme. Concentration of the enzyme is 5 micromolar. You obtained the following kinetic data: IS[ (mM) Vo, mM/s 10.83 18.57 0.02 0.04 0.07 26.76 0.1 0.15 32.50 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 What is the Km of the enzyme? O 0.1 mM 10 mM 65 mM 60 mM Which statement about the enzyme from previous question is correct? (Kinetic data are provided again just in case) IS] (mM) 0.02 Vo, mM/s 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 48.75 54.17 0.3 0.5 0.7 56.88 O Enzyme functions near catalytic perfection O Only a minor fraction of encounters between enzyme and substrate results in a reaction O Enzyme has no upper limit of catalytic efficiency O Enzyme velocity is faster than allowed by diffusion
Transcribed Image Text:Below is the set of kinetics data of a velocity of an enzymatic reaction without inhibitor (Vo) and with an inhibitor (Voi): Which one is correct about the inhibition? Vo Voi 1 0.286 0.133 0.5 0.22 0.08 0.33 0.18 0.057 0.25 0.15 0.044 0.2 0.13 0.036 O Inhibitor decreases Vmax of the enzyme O Inhibitor is most likely structurally similar to a substrate O Inhibition of the enzyme is irreversible O Inhibitor can only bind to ES complex You are studying the kinetics of an unknown enzyme. Concentration of the enzyme is 5 micromolar. You obtained the following kinetic data: IS[ (mM) Vo, mM/s 10.83 18.57 0.02 0.04 0.07 26.76 0.1 0.15 32.50 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 What is the Km of the enzyme? O 0.1 mM 10 mM 65 mM 60 mM Which statement about the enzyme from previous question is correct? (Kinetic data are provided again just in case) IS] (mM) 0.02 Vo, mM/s 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 48.75 54.17 0.3 0.5 0.7 56.88 O Enzyme functions near catalytic perfection O Only a minor fraction of encounters between enzyme and substrate results in a reaction O Enzyme has no upper limit of catalytic efficiency O Enzyme velocity is faster than allowed by diffusion
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