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The activity of an enzyme is studied with and without an inhibitor. Specifically, the initial rates are measured as a function of the concentration of substrate. Selected results are listed in the table below. The concentration of substrate is given in the first column and the rates listed in the last two columns are for experiments conducted respectively in buffer (with no inhibitor) and in a solution with the inhibitor present. S Rate (mm/min) mM Buffer Inhibitor 1.25 1.72 1.30 1.67 2.04 1.49 2.50 2.63 1.73 5.00 3.33 2.08 10.00 4.17 2.31 1. Determine the Michaelis-Menten constant, Kè, and the maximal rate, Vmax, for this reaction when there is no inhibitor. 2. State (with a reason) what type of inhibition the inhibitor studied here exerts.

The activity of an enzyme is studied with and without an inhibitor. Specifically, the initial rates are measured as a function of the concentration of substrate. Selected results are listed in the table below. The concentration of substrate is given in the first column and the rates listed in the last two columns are for experiments conducted respectively in buffer (with no inhibitor) and in a solution with the inhibitor present. S Rate (mm/min) mM Buffer Inhibitor 1.25 1.72 1.30 1.67 2.04 1.49 2.50 2.63 1.73 5.00 3.33 2.08 10.00 4.17 2.31 1. Determine the Michaelis-Menten constant, Kè, and the maximal rate, Vmax, for this reaction when there is no inhibitor. 2. State (with a reason) what type of inhibition the inhibitor studied here exerts.

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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I need help with this question. I have an exam in biological chemistery this month, so I try to be prepared. This is an exam question from last year, that I'm trying to figure out how to calculate WITHOUT using computer (its not allowed during exam). 

I will appreciate details when explaining this exercise, so I can understand it. Thank you. 

The activity of an enzyme is studied with and without an inhibitor. Specifically, the initial rates are measured as a function of the concentration of substrate. Selected results are listed in the table below. The concentration of substrate is given in the first column and the rates listed in the last two columns are for experiments conducted respectively in buffer (with no inhibitor) and in a solution with the inhibitor present. Rate (mm/min) S mM Buffer Inhibitor 1.25 1.72 1.30 1.67 2.04 1.49 2.50 2.63 1.73 5.00 3.33 2.08 10.00 4.17 2.31 1. Determine the Michaelis-Menten constant, KM, and the maximal rate, Vmax, for this reaction when there is no inhibitor. 2. State (with a reason) what type of inhibition the inhibitor studied here exerts.
Transcribed Image Text:The activity of an enzyme is studied with and without an inhibitor. Specifically, the initial rates are measured as a function of the concentration of substrate. Selected results are listed in the table below. The concentration of substrate is given in the first column and the rates listed in the last two columns are for experiments conducted respectively in buffer (with no inhibitor) and in a solution with the inhibitor present. Rate (mm/min) S mM Buffer Inhibitor 1.25 1.72 1.30 1.67 2.04 1.49 2.50 2.63 1.73 5.00 3.33 2.08 10.00 4.17 2.31 1. Determine the Michaelis-Menten constant, KM, and the maximal rate, Vmax, for this reaction when there is no inhibitor. 2. State (with a reason) what type of inhibition the inhibitor studied here exerts.
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