The image below contains a Michaelis Menten plot for an enzyme catalysed reaction. Based on this plot, estimate the Vmax and Km. Velocity, uM/sec 40 30 20 10 0 0 ENZYME CATALYSED REACTION 20 60 Substrate concentration, mM 40 Vmax = 39 umol/sec; Km = 14 mM O Vmax = 39 umol/sec; Km = 20 mM O Vmax = 14 umol/sec; Km = 39 mM O Vmax = 20 umol/sec; Km = 14 mM 80

The image below contains a Michaelis Menten plot for an enzyme catalysed reaction. Based on this plot, estimate the Vmax and Km. Velocity, uM/sec 40 30 20 10 0 0 ENZYME CATALYSED REACTION 20 60 Substrate concentration, mM 40 Vmax = 39 umol/sec; Km = 14 mM O Vmax = 39 umol/sec; Km = 20 mM O Vmax = 14 umol/sec; Km = 39 mM O Vmax = 20 umol/sec; Km = 14 mM 80

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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I-(aq) + OCI-(aq) 10-(aq) + Cl-(aq) The above reaction was studied (at a particular temperature) and the following data were obtained: [1-10 [OCI-]0 Initial Rate (mol/L) (mol/L) (mol L-1s-1) 0.360 0.100 8.42\times 10-20.045 0.100 1.05\times 10-20.090 0.200 4.21\times 10-20.180 0.200 8.42\times 10-2 Which of the following expressions for the rate law are completely consistent with the above experimental data, d[Cl-]/dt = kl OCI-][-] d[10-]/dt = k[OCI-]3 k[OCI][I] = d[OCI-]/dt-d[-]/dt = k[-]2[OC]d[1]/dt = k[-][OC] 1 pts Tries 0/5 Calculate the rate constant (k). (Units required.)
X2Y2 + 2Z + 2Y→ Z2 + 2Y2X Trial [X2Y2 ], (M) [Z], (M) [У, (М) Initial Rate (M/min) 1 0.25 0.11 0.33 0.025 0.11 0.33 0.2 3 0.25 0.66 0.33 0.15 4 0.25 0.11 0.66 0.025 A) What is the rate law? B) What is the rate constant? C) What is the initial rate if you have 0.061 M of X, 0.092 M of Y, and 0.043 M of Z?
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Consider the hypothetical enzyme-catalyzed reaction: A → B Given the kinetic data below, calculate the Vmax, in mM min-1, of the hypothetical enzyme for substrate A.
Protein phosphatase 1 (PP1) helps regulate cell division and is a possible drug target to treat certain types of cancer. The enzyme catalyzes the hydrolysis of a phosphate group from myelin basic protein (MBP). The activity of PP1 was measured in the presence and absence of the inhibitor phosphatidic acid (PA). [MBP] (mg-mL-¹) 0.010 0.015 0.025 0.050 Vo without PA (nmol-mL-¹ min-¹) 0.0209 0.0355 0.0419 0.0838 Use the data in the table to construct a Lineweaver-Burk plot. What type of inhibitor is phosphatidic acid? Uncompetitive Noncompetitive Mixed inhibition Competitive Vo with PA (nmol-mL-¹ min-¹) 0.00381 0.00620 0.00931 0.01400
Consider this initial rate data at a certain temperature in the table for the reaction OH (aq) OCI (aq) + I (aq) OI (aq) + Cl(aq) Determine the rate law. rate k [OC] (1) Answer Bank (1-1² [OH Trial 1 2 3 4 [I Jo [OCI ]o (M) [OH lo (M) (M) 0.00171 0.00171 0.510 0.00171 0.00299 0.510 0.00279 0.00171 0.643 0.00171 0.00299 0.826 [OCI"] [OH-] Initial rates (M/s) 0.000359 0.000629 0.000465 0.000388
how do we find reaction rate moles/sec using beers law? Determine the reaction rate in units of mol/sec using Beer's law. The extinction coefficient for pNP is: E = 1.8 x 10 Mcm Determine the reaction rates for the following enzyme concentration assays and enter them below. Rate for 1/2 Enzyme Concentration Rate for 2x Enzyme Concentration 2x Rare: 0.0039 Abs/see Assay 2x Rate; 0.0098 Abs/see Assy
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For an enzyme that follows Michaelis –Menten kinetics, k1=1X106 M-1 sec-1, k-1= 2x103 sec-1 and k2=2X 102 sec-1. a. What is the Km for the enzyme ? If the enzyme concentration is 10 nanomoles in 1 ml, what is Vmax for the enzyme ? What is the catalytic efficiency for this enzyme?
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Attached is the basic model for an enzyme-catalyzed reaction. Assume that substrate binding is rate determining. Write the equations for the total amount of enzyme in the reaction and the rate of the reaction. Is A or B correct? If not, show work for the correct answer A : [E] = [ES] + E B : [E] = [E]0 - [ES] ; r= k2 [E]0 S / kM + [E]
:The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics Vo (mmol/min) S (mmol/L) 0.8 3 4 217 325 433 488 1,000 :The Km for this enzyme is approximately 647 mM 4 O mM 1 O mM 1,000 Ⓒ mM 3 O mm 6 O