87-6-2-1-4590135180225 27031536040545049554058![Substrate] (nM)What is the Vmax of the enzyme data shown above?rate (nM/sec)3.

Michaelis Menton kinetics: This is well known model for Enzyme kinetics. This model relates rate of…

Answered: 8- 2- 315 405 [Substrate] (nM) 45 90…

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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3L.6.2
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
Please don't provide handwritten solution ....
8L.3.4
3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?
82.16
Find kcat for a reaction in which Vmax is 4 × 10-4 mol-min-1 and the reaction mixture contains one nanogram of enzyme. The molecular weight of the enzyme is 200,000 Da (1 Da = 1 g/mol). 2 x 10-13 min-1 2 x 10-11 min-¹ 80 min-¹ 8 x 107 min-¹ 8 x 10¹0 min-¹
8L.16.2
4.2
Please answer asap and in short
If you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM

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8- 2- 315 405 [Substrate] (nM) 45 90 135 180 225 270 360 450 495 540 58! What is the Vmax of the enzyme data shown above? 7. 6. 4. rate (nM/sec)