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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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.
A purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
In a bisubstrate reaction, a small amount of the fi rst product P is isotopically labeled (P*) and added to the enzyme and the fi rst substrate A. No B or Q is present. Will A (= P—X) become isotopically labeled (A*) if the reaction follows a Sequential mechanism?
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
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?
An uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the reaction increased by 20-fold.what is the equilibrium constant in the presence of the enzyme?
If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
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.
Describe experimental enzyme inhibition and how it leads to a deeper understanding of enzyme mechanisms. Explain mechanism-based enzyme inhibition. Describe enzyme inhibition by a transition-state analog. For fluoroacetate and hypoglcyin A, explain how each of these mechanism-based inhibitors is converted to the actual enzyme inhibitor and how this inhibitor then inhibits the relevant enzyme..
In enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complex
In a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?

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