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

Draw a hypothetical Michaelis-Menten plot for an enzyme reaction (i) without and (ii) with a pure noncompetitive inhibitor. Label Vax and Km on plot
What type of inhibition is being shown in the following graphs?
Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.
Please answer A & B attached with image.
Consider an enzyme that catalyzes the reaction S2 P, by the following simple reaction mechanism: k, E + S 2 E•S →E kcat + P Suppose the enzyme acquires a mutation that causes k1 to be 10-times smaller than for the wild-type (non-mutant) enzyme. Suppose you measure the initial reaction rate (vo) at several different [S] for the mutant and the wild-type enzymes. Under what conditions would the mutation have a greater effect on the reaction rate (vo) of the mutant enzyme compared to the wild-type enzyme - at very low [S], or at very high [S]? Explain briefly how you decided.
In the scheme below which represents the mechanism of action for a large number of enzymes: A+B⟺AB⟶C The steady state approximation is reached when: d[AB]/dt≈0 k2≫k1 k−1≫k1 k−1=k1
An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare
The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate V₁ for an enzyme-catalyzed, single-substrate reaction E + S ⇒ ES →→ E + P. The model can be more readily understood when comparing three conditions: [S] > Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity Vo where steady state conditions are assumed. [Etotal] refers to the total enzyme concentration and [Efree] refers to the concentration of free enzyme. [S] > Km Almost all active sites will be filled. Adding more S will not increase the rate. Answer Bank Not true for any of these conditions Increasing [Etotal] will lower Km.
You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE, The kinetics data are shown below [Substrate, uM] Vo with DEDS M/min) Vo without DEDS (uM/min) M3.333 10.774, 11.196 14,000 0.877 1.316 5.000 1.012 #1.462 10.000 1.462 088'1 20.000 1.880 12198 Using linear regression analysis. deterane tievaluesof Vun K orthe ercymehine ABSENCE of inhibitoe Express your answer In 3 decimal places, do NOT include the units)
(i) Which graph indicates an enzymatic reaction without inhibitor?(ii) Which type of inhibitor is it? Briefly explain.(iii) Which graph indicates the highest concentration of inhibitor?(iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers.
Can you graph the data
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.

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