ANSWER C AND D PLS You are in the laboratory and measure the initial rate of an enzyme reaction as a function of substrateconcentration in the presence and absence of an inhibitor. You obtain the following data:[Substrate], mMVo, - inhibitor,(μM/min)Vo, + inhibitor,(μM/min)0.000133170.000250290.000571500.00183670.00291800.00596910.0198950.0299980.05100990.11001000.1100100 (c) When [S] = 0.0004, what will Vo be in the absence of inhibitor?(d) When [S] = 0.0004, what will Vo be in the presence of inhibitor?

Km is the MM constant which is used as an affinity measurement for an enzyme. Km is equal to the…

Answered: (c) When [S] = 0.0004, what will Vo be…

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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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?
A researcher has measured the initial rate of an enzyme-catalyzed reaction as a function of substrate concentration in the presence and absence of 0.001μM inhibitor. She obtains the following data. What is the Vmax and Km for the "no inhibitor" and "+ inhibitor" experiments. Ans, What would be value of V0 for the "+inhibitor" at [S] = 0.4μM and the inhibitor is most likely a competitive, uncompetitive or mixed inhibitor.
Refer to the following graph when answering questions. These words may be used to fill: competitive, uncompetitive, noncompetitive, irreversible. -1 mg , μmol min-1 v-1 0.2 0.1 THA -4-2 CBA + 2 4 [S]-1, (mM-1) Word 1, The value of Km for the enzyme depicted by curve A is 2, The value of Vmax for the enzyme depicted by curve A is 3, Curve B depicts the effect of an inhibitor on the system described by curve A. This inhibitor is a inhibitor. 4, Curve C depicts the effect of a different inhibitor of the system described by curve A. This second inhibitor is a inhibitor. D
Please use the graph below to explain the differences between the 2 enzymes whose activities are plotted (enzyme 1-blue and enzyme 2-red). Using appropriate biochemical terminology, how do these differences affect the activity and function of Enzyme 1 versus Enzyme 2? Reaction velocity (vo) Vmax Vmax 2 0 0 Enzyme 1 Enzyme 2 [Substrate]
A hollow fiber enzyme reactor (HFER) consists of 5000 fibers. Each fiber has an internal diameter of 0.04 cm, and on the inside surface of the fibers, an enzyme has been immobilized that removes a toxin from plasma that is flowing through the inside of the fibers. The enzyme reaction is very fast, so a reasonable assumption is that the concentration of the toxin at the surface of the hollow fiber is equal to zero. The /HFER operates at 37°C, and the plasma enters at a total flow rate of 200 mL/min. The concentration of the toxin in the plasma that enters the HFER is 1 mg/L, and its MW is 636 g/mol. If the fibers in the HFER are 50 cm in length, what is the concentration of the toxin in the plasma as it leaves the HFER?
You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatase
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 Vmax value for this reaction. Report your answer to four significant figures in units of 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 kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
Draw three different Lineweaver-Burke plots for an enzyme in the presence or absence of a (1) competitive inhibitor, (2) uncompetitive inhibitor, (3) noncompetitive inhibitor. Indicate on your graphs: Vmax, max (app), Km and Km (app) for each case.
s) In two experiments carried out in a research lab, an enzyme reaction is run with and without an inhibitor. Samples were taken over time to measure the concentration of product as the reaction proceeds, with raw data given below. Data were collected at 34 °C and pH 7.5, using [S] = 0.115 M (for both trials) & [E], = 0.0024 M (for both trials): Product concentration (mol P/L) No inhibitor [1] = 0.019 M 0 0 0.0011 0.0023 0.0031 0.0045 0.0074 0.0119 0.0195 0.0271 0.0410 0.0479 0.0550 0.0588 0.0600 Time min 0 3.5 9 13 17 26 43 69 104 156 208 311 415 519 0.0016 0.0038 0.0052 0.0078 0.0111 0.0180 0.0281 0.0412 0.0525 0.0587 0.0598 0.0600 0.0600 A. Determine the initial reaction velocities for both reactions. B. From these data, can you determine what type of inhibition is occurring? If so, show evidence of the type of inhibition occurring. If not, describe what experiment(s) should be done to determine the type of inhibition (competitive, non-competitive or uncompetitive), as well as how…
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
Draw the Michaelis-Menten Plot and Lineweaver-Burke Plot of an enzyme in thefollowing situation. An enzyme, Enzyme A, has an optimal temperature at 34.5oC. The enzyme kinetic parameters were recorded to be Km = 15.0 μM, Vmax = 12.0 μM/s. The condition for an enzyme kinetic experiment has the temperature raised to 36.5oC. What will happen to the results? Provide at least five data sets prior to raising the temperature and after raising the temperature and plot the graphs as overlaying figures for comparison. Explain youranswer using a minimum of 200 words.

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(c) When [S] = 0.0004, what will Vo be in the absence of inhibitor? (d) When [S] = 0.0004, what will Vo be in the presence of inhibitor?