Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs. The given image is a Lineweaver-Burk plot, which is used to determine the kinetic parameters of an enzyme that follows Michaelis-Menten kinetics. The graph is a double-reciprocal plot where the y-axis represents \( \frac{1}{v} \) (inverse of reaction velocity in mmol/sec) and the x-axis represents \( \frac{1}{[S]} \) (inverse of substrate concentration in mM).The equation of the line is given as:\[ y = 0.5032x + 0.0516 \]This equation is in the form of a straight line \( y = mx + b \), where:- \( m \) (slope) = 0.5032 - \( b \) (y-intercept) = 0.0516To find the maximum velocity (\( V_{max} \)) and the Michaelis constant (\( K_m \)):- \( V_{max} \) is the reciprocal of the y-intercept (\( b \)): \[ V_{max} = \frac{1}{0.0516} \] - \( K_m \) can be calculated using the slope (\( m \)) and \( V_{max} \): \[ K_m = \text{slope} \times V_{max} = 0.5032 \times V_{max} \]These calculations will give the values of \( V_{max} \) and \( K_m \) with two significant figures.

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Answered: 5.4 Give the Vmax and Km for this…

5.4 Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs. 0.6 y = 0.5032x + 0.0516 0.5 0.4 0.3 0.2 0.1 -0.4 -0.2 0.2 0.4 0.6 0.8 1 -0.1 1/[S] (mM) 1/v (mmol/sec)

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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5. An enzyme catalyzes the reaction M concentration of 1 nM, and the Vmax is 2 µM s-1. The Km for substrate M is 4 µM. N. The enzyme is present at a (a) Calculate kcat. (b) What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 2.0? Increased or decreased?
Enzyme X can act on either substrate A or B; the Km on A < Km on B. Vmax for A > Vmax on B.Sketch 1 plot for 1/v vs. 1/[S] plot for Enzyme X in the presence of A and in the presence of B.
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Let's try similar things with another enzyme! Here's one with a cool mechanism that makes an interesting product. Cys157 Cys157 Cys157 His296 His296 His296 OH HNN: HN, HN -CO2 CH2 Asn329 Asn329 Asn329- Cys157 His296 OH OH HNNH HC. Asn329 N Note that this figure is typical of those found in the biochemical literature in that it provides a somewhat abbreviated view of what is happening. For example, the arrows I have circled in red above for the fırst step need some sorting out. What mechanism is represented by these arrows? O a two step, addition/elimination reaction O an SN2 reaction O an SN1 reaction O nucleophilic aromatic substitution O electrophilic aromatic substitution
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