what is the Vmax and Km of the enzyme in the reaction asap please. The enzyme that creates prostaglandins (lipids that enable inflammation at sites of injury) uses arachidonic acid as a substrate to form PGG₂. You perform an experiment and obtain the following data.[arachidonic acid] (mm)rate of PGG2 formation (mM/s)0.511.52.53.51/rate of PGG2 formation (s/mM)-1.5-1-0.50.05Which you then plot into the following Lineweaver Burk plot.y = 0.0116x + 0.01940.040.03F0.020.010.511/[arachidonic acid] (1/mM)23.5032.236.941.8441.522.5

Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Answered: what is the Vmax and Km of the 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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The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. Morphine is a non-competitive inhibitor of carbonic anhydrase. Draw on the same Lineweaver-Burke plot as above a graph showing the effect of a concentration of morphine that inhibits the first enzyme such that it reduces the Vmax to ½ its maximal value. Make sure to put in sample data points. Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.
Sketch a typical enzyme kinetic curve of [S] vs. V. The maximum [S] should be about four times the Km. Draw lines at [S] = Km and V = Vmax. Draw the asymptote at [S] = 0.
An enzyme catalyzes a reaction with a K of 7.50 mM and a Vmax of 4.15 mMs. Calculate the reaction velocity, o, for each substrate concentration. [S] = 1.75 mM MM-s-1 [S] = 7.50 mM [S] = 11.0 mM DO mM-s mM-s
Many enzyme -catalyzed reactions are consistent with a modified version of the Michaelis -Menten mechanism in which the second step is also reversible. For this mechanism obtain an expression for the rate of formation of product and find its limiting behavior for large and small concentrations of substrate using steady state approximation
The reaction: A + B <-> P + Q is catalysed by enzyme E. Draw a Cleland diagram for a Non-sequential (Ping-Pong) mechanism for this reaction.
An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min−110 µmol⋅min−1 when the substrate concentration is five times greater than the ?M.KM. What is the ?maxVmax of this enzyme?
Distinguish between the concerted and sequential models for the behavior of allosteric enzymes. Give 2 differences
How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.
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.
Please answer this question and the highlighted question is wrong please explain why and give me the correct answer
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
How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s

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