The enzyme triosephosphate isomerase (TIM) catalyzes the following reaction in glycolysis,where it converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (GAP).CH₂OHC=OCH₂OPO²-DHAPtriose phosphateisomerase[DHAP] (MM1.002.003.006.00OV. (mM/s)3.7006.7279.25014.800=HHCOHCH₂OPO²-Kinetics experiments were performed on TIM. Enzyme activity (initial velocity, V.) was measuredat varying concentrations of DHAP. The enzyme kinetics were also measured in the presence oftwo inhibitors, A and B. The enzyme concentration used in all experiments was 25.00 μM. Thedata are shown below.GAPV. (mM/s) + A1.4522.7944.0387.281V₁ (mM/s) + B0.7551.3791.9053.077 1. For the uninhibited enzyme, calculate the slope and y-intercept of the Lineweaver-Burkgraph.2. Calculate values of Km and Vmax for TIM.3. How long (in seconds) does a single catalytic event take?4. What will be the V, at 9.00 mM [DHAP] and 25.00 µM [TIM]?

To solve all the 4 questions, we need to draw the Lineweaver Burk (LB) plot in the absence of…

Answered: 1. For the uninhibited enzyme,…

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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6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.
Most of the enzyme reactions followed the mathematical kinetic plots suggested by the Michaelis-Menten plots:viii. Draw another Lineweaver-Burk plot and on the same plot, draw a graphto indicate un-competitive inhibition.Note: In the graphs, lable Vmax and KM clearly.
For an enzyme-catalyzed reaction, the velocity was determined at two different concentrations of the substrate. Estimate the value of Vmax. [S] (MM) 10 20 88 nmol/min 79 nmol/min 67 nmol/min V(nmol/min) 51 nmol/min 27 Not enough information is given to form a reasonable estimation. 48
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
Two enzyme catalyzed reactions, RA (red) and Rp (blue), have kinetic profiles shown below. Report which reaction has the higher maximal rate and which reaction has the smaller Km. в A 1/ [S] Higher Vm [ Select ] Lower Km [ Select ] A/T
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
From the chart below, comment on the temperature dependence of this enzyme catalyzed reaction.
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
V 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km. Estimate the Km from this graph giving the correct units. v/Vmax 1.0 0.5 0.0 0.0 vs [S] for an enzyme. Enzyme Activity vs [Substrate] :0.2 0.4 Substrate (HM): 0.6 (b) If the Vmax = 25 mmoles per minute per µmole of enzyme calculate the Keat and the specificity constant."
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain

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1. For the uninhibited enzyme, calculate the slope and y-intercept of the Lineweaver-Burk graph. 2. Calculate values of Km and Vmax for TIM. 3. How long (in seconds) does a single catalytic event take? 4. What will be the V, at 9.00 mM [DHAP] and 25.00 µM [TIM]?