O(a) 1x1010; (b) 1x104/s(a) 1.25x10-5; (b) 5x10-11/sO(a) 1x1010; (b) 5x10-11/sO(a) 2x1014; (b) 1.25x10-5(a) 2x10-14; (b) 1x104/s In an uncatalyzed reaction, KF(uncatalyzed) = 2.5 X 10-8/s and Keq is 5 X 10².For the same reaction in the presence of an enzyme, KF(catalyzed) = 2.5 X10²/s.Remember that Keq = KF/KR = k₁/k-1.(a) What is the rate enhancement of the catalyzed reaction in the forwarddirection?(b) What is the value for KR(uncatalyzed)?

Consider the reversible reaction given below. A ⇄kRkF B Here , kF is the rate constant for the…

Answered: In an uncatalyzed reaction,…

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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Similar questions

At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
An uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the reaction increased by 20-fold.what is the equilibrium constant in the presence of the enzyme?
In enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.
If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?
For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.
What is the impact of new km value 0.1mM compared to previous km value 0.05mM on affinity of the enzyme for substrate?
List 4 major types of inhibition modes and clearly indicate the effect on Vmax and KM for each mode?2. What is the effect of each of the 4 types of inhibitors on the initial rate of an enzyme catalyzed reaction?3. A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?4. Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.
Given the following data in enzyme-catalyzed reaction, what is the Vm, Km and type of inhibition of Experiment A?
At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?

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