### Understanding the Michaelis-Menten PlotTo improve comprehension of enzyme kinetics, refer to the Michaelis-Menten plot to answer the following question. **Question:**What is the estimated value of Vmax for the enzyme-catalyzed reaction (square data points)? *(Choose the one best answer)*- ○ 30 mM- ○ 30 mM/sec- ○ 60 mM/sec- ○ 60 mMBefore answering, recall that Vmax is the maximum rate at which an enzyme can catalyze a reaction when fully saturated with substrate. Refer to the accompanying Michaelis-Menten plot provided in your materials for detailed data points.---*Page Navigation:*- Previous Page- Next Page *Page:* 20 of 36 ### Michaelis-Menten Plot Analysis#### Graph DescriptionThe displayed graph is a Michaelis-Menten plot that depicts the relationship between substrate concentration and the initial velocity (Vo) of an enzyme-catalyzed reaction. The x-axis represents the substrate concentration in millimolar (mM), and the y-axis represents the initial velocity (Vo) in mM/sec.- **X-axis (Substrate in mM)**: Begins at 0 and goes up to 300 mM.- **Y-axis (Vo in mM/sec)**: Starts at 0 and progresses up to 60 mM/sec.- **Data Points**: Square data points are plotted to show the relationship between the substrate concentration and the enzyme reaction velocity.The graph shows a classic hyperbolic curve which is typical for Michaelis-Menten kinetics. As the substrate concentration increases, the reaction velocity rises rapidly at first and then approaches a maximum velocity (Vmax) asymptotically.#### Educational TextUse the Michaelis-Menten plot to answer this question: **What is the estimated value of Vmax of the enzyme-catalyzed reaction (square data points)?** (Choose the one best answer)Based on the graph, it is observed that the reaction velocity (Vo) levels off as substrate concentration increases, approaching a maximum value. To estimate Vmax from the Michaelis-Menten plot, identify the asymptote (the horizontal line the curve approaches but never quite reaches) on the y-axis.This graphical representation is crucial for understanding enzyme kinetics and determining vital parameters such as Vmax and Km (Michaelis constant), helping elucidate the catalytic efficiency and affinity of enzymes for their substrates.

Vmax : Reaction rate- when the enzyme gets fully occupied by substrate. Vmax- Maximum velocity

Answered: Use the Michaelis-Menten plot to answer…

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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You find in the literature that an enzyme purified very close to homogeneity has a specific activity of 12,300 U/mg. What is likely to be the largest source of error in the quoted value? U (unit) typically is defined as the amount of enzyme that is required to consume 1.00 umoles of substrate per minute under some given set of conditions. Units are typically determined spectrophotometrically by measuring the rate of formation of product.
The following data were collected for an enzyme that can be described by Michaelis Menton kinetics. Use graphical analysis to determine the Km and Vmax for this exzyme / substrate combination. [S] mM Product formed (umol/min) 0.21 1.5 2.0 0.24 3.0 0.28 4.0 0.33 8.0 0.40 16.0 0.45
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. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
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Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the above enzyme (lactase). (enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 per minute 0.25 per minute 0.50 per minute 1.25 per minute 5.0 per minute
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Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the enzyme catalyzed reaction (square data points)? (choose the one best answer) 30 mM 30 mm/sec 60 mm/sec 60 mM Previous Page Page 20 of 36 ha Next Page