(1) Vo (uM.S (2) Vo (3) Vo (mM) 0.77 1 2.5 1.17 2 4.0 2.10 1.25 5 6.3 4.00 2.00 2.50 10 7.6 5.7 20 9.0 7.2 2.86

Chemistry: Principles and Reactions
8th Edition
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:William L. Masterton, Cecile N. Hurley
Chapter7: Covalent Bonding
Section: Chapter Questions
Problem 5QAP: Follow the directions of Question 1 for (a) OCl2 (b) PF3 (c) SbCl6- (d) ICl4-
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The following table indicates the rates at which a substrate reacts as catalyzed by an enzyme that follows the Michaelis-Menten mechanism: (1) in the absence of inhibitor; (2) and (3) in the presence of 10 mM concentration, respectively, of either of two inhibitors. Assume [E]T is the same for all reactions.

(a) Determine KM and Vmax for the enzyme. For each inhibitor determine the type of inhibition and KI and/or K’I. What additional information would be required to calculate the turnover number of the enzyme? (b) For [S] = 5 mM, what fraction of the enzyme molecules have a bound substrate in the absence of inhibitor, in the presence of 10 mM inhibitor of type (2), and in the presence of 10 mM inhibitor of type (3)?

(1) Vo
(uM.S
(2) Vo
(3) Vo
(mM)
0.77
1
2.5
1.17
2
4.0
2.10
1.25
5
6.3
4.00
2.00
2.50
10
7.6
5.7
20
9.0
7.2
2.86
Transcribed Image Text:(1) Vo (uM.S (2) Vo (3) Vo (mM) 0.77 1 2.5 1.17 2 4.0 2.10 1.25 5 6.3 4.00 2.00 2.50 10 7.6 5.7 20 9.0 7.2 2.86
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