Macmillan LearningN.XConsider the data collected for an enzyme-catalyzed reaction.% (mM-s¯¹)0.370.832.223.08F2Determine Vmax and Km for this reaction.# 3#EDVmaxKm -F3[S] (mM)0.200.502.004.00JANMAN!$4PERNIERF3.08IncorrectV14-IncorrectFA%5TGBHOL6F5YH&7NF6UJ8DELLF7NK9F8O>F9PWF10{?[1F11}1F12BackspaceEnterShiftInsertPrintScreenDeleteHomeScrollLockEndⒸ Attempt 18:26 PM10/15/2023+PgUpPauseBreakPgDnmM-s-lmMGNumLock7Home481EndST5O

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: Macmillan Consider the data collected…

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 accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried out in the presence, or absence, of aninhibitor. Indicate what type of inhibition is predicted based on eachLineweaver–Burk plot. For each plot indicate which line corresponds to thereaction without inhibitor and which line corresponds to the reaction withinhibitor present.
Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minute
Given the initial rate data for the reaction A + B → C, determine the rate expression for the reaction. [A], M [B], M A[C]/At (initial) M/s 0.0418 0.122 2.73 x 10-4 0.0836 0.122 10.9 × 10 4 0.0418 0.488 2.73 x 104 O A[C] At ○ A[C] ΔΙ = 0.439 Ms[A][B]² = 1.27 M²s¹ [A][B] ● A[C] = 6.53 × 10³ s¹ [A] At O A[C] = 0.156 M's¹[A]² At ○ A[C] At = 5.35 x 102 M2s[A][B]
can you explain what is happening in the attached graph? Figure 3: Lineweaver-Burke plot of alkaline phosphatase activity without inhibitor
For an enzyme that has a Km of 25 mM, Vmax of 50 mM/s and kcat of 250 s-1, how long does a single reaction take? Select one: 50 ms 250 ms 4 ms 25 s 4 s
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
Compound A is the substrate for two enzymes, El and E2, their reaction rates, r1 and r2,Determine the Km and rmax for both enzymes, with respect to the concentration of A. Which set of data is more likely to be for El and which for E2, and why? Concentration of 0.2 0.6 1.2 3 4 5 6 8 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
Please answer asap and in short
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
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
The following data have been obtained for two different initial enzyme concentrations for an enzyme-catalyzed reaction. [E]=0.015 g/l) (g/l-min) [S] (g/l) v([E]=0.00875 g/l) (g/l-min) 1.14 20.0 0.67 0.87 10.0 0.51 0.70 6.7 0.41 0.59 5.0 0.34 0.50 4.0 0.29 0.44 3.3 0.39 2.9 0.35 2.5 a. Find K b. Find V for [E]=0.015 g/l. c. Find V for [E]=0.00875 g/l. d. Find k2. Use Eddie-Hostee plot to find your answer. Compare your result using Hanes- Wolf plot.

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Macmillan Consider the data collected for an enzyme-catalyzed reaction. % (mM-s-¹) 0.37 0.83 2.22 3.08 [S] (MM) 0.20 0.50 2.00 4.00 Determine Vmax and Km for this reaction.