E17F.5(b) The enzyme-catalysed conversion of a substrate at 298 K has K 0.032mol dm and 425x10 mol dm when the enzyme concentration is 3.60 x 10 mol dm. Calculate the catalytic efficiency of the enzyme, as defined in Exercise E17F.5(a) wwwwam ES ES vk,[ES ES'E+P vkES] Show that the rate of formation of product has the same form as that shown in eqn 17F.16, but with and K given by k (k+k) sk(kk) kkE К, ktk www

E17F.5(b) The enzyme-catalysed conversion of a substrate at 298 K has K 0.032mol dm and 425x10 mol dm when the enzyme concentration is 3.60 x 10 mol dm. Calculate the catalytic efficiency of the enzyme, as defined in Exercise E17F.5(a) wwwwam ES ES vk,[ES ES'E+P vkES] Show that the rate of formation of product has the same form as that shown in eqn 17F.16, but with and K given by k (k+k) sk(kk) kkE К, ktk www

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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A certain enzymatic reaction is found to be zero ordeth respect to the substrate being converted. The rate constant for the reaction is found to be 540 M s-1. The initial concentration of the substrate is 0.350 M. When the reaction is 50% complete, what is the rate of the reaction at that point? Give your answer in M s1 but do not include units in your answer.
28. Calculate the velocity of an enzyme- catalyzed reaction A+B P+Q at [A]= 2x 10 M and [B]= 6.7x 10 M. Assume that A and B add randomly to the enzyme and (a) a =1 (the binding of one substrate has no effect on the binding of the other), (b) a 0.1 (the binding of one substrate decreases the %3D
For a simple reaction, S 1 P, k1 is the rate of the forward reaction and k-1 is the rate of the backwards reaction. The k1 in the absence of any enzyme was 0.01/s. The k1 in the presence of enzyme was 5,000,000/s. Calculate the rate enhancement (k1 catalyzed divided by k1 uncatalyzed) provided by the enzyme. If the equilibrium constant in the absence of enzyme is 1 x 104, what is the equilibrium constant (Keq) in the presence of enzyme?
Answer Q35, 36, 37
3a
In a study of the decomposition of nitramide in aqueous solution at 25 °C NH2NO2(aq)N20(g) + H20(1) the concentration of NH2NO2 was followed as a function of time. It was found that a graph of In[NH,NO2] versus time in seconds gave a straight line with a slope of -6.72x105 s and a y-intercept of -0.911 . Based on this plot, the reaction is | reaction is |order in NH2NO2 and the half life for the seconds.
Regarding the activated complex, it can be stated that: (I) Its existence is fleeting, as long as the reaction takes place, but it disappears when it ends. (II) It is easily observable in any reaction. (III) It has the same properties as a reaction intermediate. (IV) It is simply the point of maximum energy in the corresponding reaction energy profile.
What is the function of the enzyme lactase?
The data in the table below describe an enzymatic reaction. The relative molecular mass of the enzyme is 50000 g/mol and its concentration is 2 x 103 g/cm. Determine the rate constant for the breakdown of the enzyme substrate intermediate from the data given in table. Enzymatic rate data [substrate] (M) initial rate/Ms 13 4 20 29 12 33 16 36 20 38 Hiterh: 22. 000
2. Enzyme-catalysed reactions are sometimes subject to inhibition by the substrate. Assuming that the reaction mechanism can be approximated by the following model, derive an expression for the reaction velocity in terms of S, Eo and reaction constants. State your assumptions. Dissociation constant E +S S ES K, ES + S S ESS K,' k ES - E+P
Show that if it can be assumed that there is a pre-equilibrium involving step (1), the rate of formation of ethylene oxide is v = k,K[CH,CICH,OH][OH ], where K is the equilibrium constant for the first step and k, is the rate constant for the second step. E17E.2(b) 'The mechanism for the reaction between 2-chloroethanol, CH,CICH,OH, and hydroxide ions in aqueous solution to form ethylene oxide, (CH,CH,)0, is thought to consist of the steps (1) CH,CICH,OH+OH 2CH,CICH,O¯+H,O (2) CH,CICH,O¯ –→(CH,CH,)O+CI