Problem 13 of 15SubmitUsing the following reaction datapoints, construct Lineweaver-Burkplots for an enzyme with and withoutan inhibitor by dragging the points totheir relevant coordinates on thegraph and drawing a line of best fit.Using the information from this plot,determine the type of inhibitorpresent.1mM-11s mM-1[S]'V'with 10 μg per20541036205272.5231.2520Answer:||| Problem 13 of 15SubmitUsing the following reaction datapoints, construct Lineweaver-Burkplots for an enzyme with and withoutan inhibitor by dragging the points totheir relevant coordinates on thegraph and drawing a line of best fit.Using the information from this plot,determine the type of inhibitorpresent.with 10 μg per mL inhibitor1s μM-1V'Answer:|||7254454138

The Lineweaver-Burk plot is a way to analyze enzyme activity by plotting the reciprocal of the…

Answered: Problem 13 of 15 Submit Using the…

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter6: The Behavior Of Proteins: Enzymes

Section: Chapter Questions

Problem 60RE

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Similar questions

MATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?
MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
MATHEMATICAL You do an enzyme kinetic experiment and calculate a Vmax of 100 mol of product per minute. If each assay used 0.1 mL of an enzyme solution that had a concentration of 0.2 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol?
MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KM
MATHEMATICAL The standard free-energy change for the reaction Arginine+ATPPhosphoarginine+ADP is +1.7kJmol1. From this information and that in Table 15.1, calculate the G for the reaction Phosphoarginine+H2OArginine+Pi
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
MATHEMATICAL The free-energy change (G) for the oxidation of the cytochrome aa3 complex by molecular oxygen is 2102.3kJ=224.5kcal for each mole of electron pairs transferred. What is the maximum number of moles of ATP that could be produced in the process? How many moles of ATP are actually produced? What is the efficiency of the process, expressed as a percentage?
MATHEMATICAL The G for the reaction Citrate Isocitrare is +6.64kJmol1=+1.59kcalmol1. The G for the reaction Isocitrate -Ketoglutrate is 267kJmol1=63.9kcalmol1. What is the G for the conversion of citrate to - ketoglutarate? Is that reaction exergonic or endergonic, and why?
On a molecular level, how can endotherms produce their own heat by adjusting processes associated with cellular respiration? If needed, review Ch. 7 for details on respiration.
REFLECT AND APPLY The enzyme lactate dehydrogenase catalyzes the reaction Pyruvate+NADH+H+lactate+NAD+ NADH absorbs light at 340 nm in the near-ultraviolet region of the electromagnetic spectrum, but NAD1 does not. Suggest an experimental method for following the rate of this reaction, assuming that you have available a spectrophotometer capable of measuring light at this wavelength.
MATHEMATICAL Using the information in Table 20.2, calculate G for the following reaction: 2Cytaa3[oxidized;Fe(III)]+2Cytb[reduced;Fe(II)]2Cytaa3[reduced;Fe(II)]+2Cytb[oxidized;Fe(III)]
MATHEMATICAL For the following aspartase reaction (see Question 28) in the presence of the inhibitor hydroxymethylaspartate, determine KM and whether the inhibition is competitive or noncompetitive. [s](molarity)V,noInhibitor(arbitraryunits)V,InhibitorPresent(samearbitraryunits)110451041.5103510311.00.0260.0920.1360.1659.520.0100.0400.0860.1427.60

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