Please help with all three parts of question 2C Two homologues of this enzyme from different species both catalyze the reaction SY with distinct Km values.Protein A catalyzes the reaction with Km = 2.0 μM and protein B catalyzes it with Km = 0.5 µM. In an experiment whereeach enzyme is mixed with 1 μM substrate, the plot of product Y formation over time was obtained. Which curvecorresponds to which enzyme?Time2D How could we use experiments like the experiment above to determine the Km and Vmax of other homologousenzymes?2E If a competitive inhibitor with K₁=2 µM were added to a homolog of an enzyme with Km = 2 mM, what would be theresulting Kmapparent?[X]

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Answered: 2C Two homologues of this enzyme from…

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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Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM s–1. EnzymeB catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM s–1. When 100 μM ofS is added to a mixture containing equal amounts of enzymes A and B, which reaction product (Por Q) will be more abundant after 1 minute of reaction?
The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?
An enzyme with a Km of 3 X 10-4 M was tested at an initial substrate concentration of 10-5 M. In 1 minute, 5% of the substrate was found to be utilized. (a) What percentage of the substrate was utilized in 5 minutes? (b) If the initial substrate concentration had been 8 X 10-7 M, what percentage of the substrate would have been utilized in 5 minutes? (c) Vmax =? (d) How long would it take to utilize 50% of the substrate at 8 X 10-7 M? (e) How long would it take to utilize 75% of the substrate at 10-5 M?
Enzyme X has a molecular weight of 48,000. It converts substrate Z into product Y. Z absorbs at 340 nm, and Y absorbs at 480 nm. A.) At what wavelength would you measure the change in absorbance to assay for enzyme X? Would the absorbance increase or decrease over time? B.)If Vmax = 60 μmol/min and you used 400 μL of a 0.1 mg/mL solution of enzyme, what is the turnover number?
You have been researching two additional methyltransferase enzymes that catalyze the same reaction. At a concentration of 10 nMoles enzyme, Enzyme A has a Km of 60 mmol, while Enzyme B has a Km of 2 mmol for the reaction conditions. You have two solutions (A and B) with equal amounts of Enzyme A in tube A and Enzyme B in tube B respectively. They both have the same Vmax of 500 mmol/second. Which enzyme would have a higher reaction velocity with the substrate concentration of 30 mmol? Why? Give approximate reaction velocity values for each enzyme (mmol/s) Would this result change if the substrate was 1000 and 1,000,000 mmol? Explain why, and give approximate reaction velocity concentrations. An irreversible inhibitor has been added to the reaction mixes A and B. It binds with 100% affinity for Enzyme A, but does not bind to Enzyme B. If 5 nMoles of inhibitor is added to the reaction, what would happen to the apparent Km and Vmax of Enzyme A and B?
Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM ∙ s−1. Enzyme B catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM ∙ s−1. When 100 μM of S is added to a mixture containing equivalent amounts of enzymes A and B, after 1 minute which reaction product will be more abundant: P or Q?
You receive kinetic data for a transferase reaction where AX and B are substrates, while A and BX are products. You are asked to establish the reaction mechanism. Which graph will you draw first? A,B,C or D A. 1/Vo against [AXo] at different concentrations of [BXo] B. 1/[AXo] against 1/[Bo] at different concentrations of [BXo] C. 1/Vo against 1/[AXo] at different concentrations of [Bo] / D. 1/Vo against 1/[AXo] at different concentrations of [1/BXo]
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
You wish to separate and purify enzyme A from contaminating enzymes B and C. Enzyme A is found in the matrix of the mitochondria. Enzyme B is embedded in the mitochondrial membrane, and enzyme C is found in the peroxisome. Enzymes A and B have molecular weights of 60,000 Da. Enzyme C has a molecular weight of 100,000 Da. Enzyme A has a pI of 6.5. Enzymes B and C have pI values of 7.5. Design an experiment to separate enzyme A from the other two enzymes.
Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share the same value for Vmax. Using this information, can you derive conclusions how the km values for enzymes A and B compare to each other?
An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.
A catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. Ea

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