Based on the following plot, the KM for Enzyme A (shown in red) is type your answer... mM If this plot was generated using 10 μM of each enzyme in the reactions whose initial velocities are plotted above, which enzyme has the highest substrate specificity? Enter the lower case letter from the options below only. type your answer... a. Enzyme A b. Enzyme B c. They both have equal substrate affinity d. Cannot be determined based on information given.

Based on the following plot, the KM for Enzyme A (shown in red) is type your answer... mM If this plot was generated using 10 μM of each enzyme in the reactions whose initial velocities are plotted above, which enzyme has the highest substrate specificity? Enter the lower case letter from the options below only. type your answer... a. Enzyme A b. Enzyme B c. They both have equal substrate affinity d. Cannot be determined based on information given.

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.2E: List two ways that enzyme catalysis of a reaction is superior to normal conditions.

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Similar questions

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2.1. For an enzyme (5µM), the following initial velocities have been reported depending on the substrate concentration: [Substrate], mM Vo 0.02 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 2.2. Sketch the Eadie-Hofstee plot for the enzyme reaction 2.3. Determine Km and Vmax for this enzyme 2.4. Indicate where Vmax and Km can be recognized
What should be taken in consideration when designing an enzyme kinetics experiment so that the reaction will not be too slow or too fast? M - amount of substrate B - amount of enzyme |- temperature O - pH
The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.
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Given the following data for an enzyme-catalyzed reaction. Substrate conc., mM Velocity, mM/s 0.10 0.96 o.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.00 2.63 1.Write the equation of the line consistent with the Lineweaver- Burke equation (type answer in this format: y=mx+b) 2. Calculate the Vmax. 3. Calculate the Km. Please help me. Kindly explain step by step the solution to this problem. Thank you.
The following results were obtained for an enzyme-catalyzed reaction Substrate concentration (mmol 1-¹) 5.0 6.67 10.0 20.0 40.0 Initial velocity (μmol l-¹ min-¹) 147 182 233 323 400 Calculate K and Vmax
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a. Using the graph paper below, to plot the enzyme velocity versus the substrate concentration in the absence of ibuprofen, estimate the Km and Vmax for this enzyme.
Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation. a)At what substrate concentration would an enzyme with a kcatof 30.0 s-1and a Kmof 0.0050 M operate at one-quarter of its maximum rate? b)Determine the fraction of Vmax that would be obtained at the following substrate concentrations [S]:1/2Km,2Km,and10Km. c)An enzyme that catalyzes the reaction X ßàY is isolated from two bacterial species. The enzymes have the same Vmax, but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, while enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X]=1 μM. Which curve corresponds to which enzyme?