Initial rates of an enzyme -catalysed reaction at different substrate concentrations are listed in Table 2.1s, mol/L0.00410.000950.000520.0001030.000049v, mol/(L. min) x 10°177173125106800.00001060.0000051a) Evaluate K and vmax by a Lineweaver-Burk plotb) Using the Eadie-Hofstee plot, evaluate K and Vmaxc) Using theHanes-Woolf plot, evaluate K and Vmaxd) Comment on the accuracy of the three methods6743E

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Answered: Initial rates of an enzyme -catalysed…

Chemical Principles in the Laboratory

11th Edition

ISBN:9781305264434

Author:Emil Slowinski, Wayne C. Wolsey, Robert Rossi

Publisher:Emil Slowinski, Wayne C. Wolsey, Robert Rossi

Chapter21: Rates Of Chemical Reactions, Ii. A Clock Reaction

Section: Chapter Questions

Problem 2ASA

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For an enzyme -catalyzed reaction, KM=10.0 mmol dm-3, vmax=0.250 mmol dm²³ s-'; [E]o= 2.3 x 10-6 mmol dm-3. Calculate the catalytic efficiency (=kb/KM) of the enzyme. 0.920 dm³ mol-l s-1 3.1 x 107 dm³ mol-1 s-1 1.1 x107 dm³ mol-l s-1 0.250 dm³ mol-l s-1
The active form of the enzyme alcohol dehydrogenase exists as a homotetramer (MW = 150 kDa), and has one identical active site located on each of its four subunits. You have performed a series of enzyme kinetic experiments using 0.025 mL of an enzyme sample that is 4.0 pg/mL and determined that the following Vmax = 2.442 x 10-2umoles/min What is the turnover number of this enzyme (in units of #/sec)? 76/ sec 305 / sec 152 / sec 4579/ sec 1526 / sec O O O O
Using the kinetic data pictured, estimate Vmax and Km for the catalysis of Substrate 1 by the following enzyme (using the correct units).
The initial velocity catalyzed by Enzyme A (red) and Enzyme B (gray) for the same substrate is plotted below as a double reciprocal plot. For the following data - answer each of the fill-in-the-blank questions. -0.75 1/Vo (min/mm) 0.5+ 0.4+ 0.3 0.2- 0.1 -0.25 0.5 A 1.0 + 1/[S] (1/mM)
The enzyme-catalysed conversion of a substrate at 25 oC has a Michaelis constant of 0.015 mol dm-3 . and a max-imum velocity of 4.25 x 10-4 mol dm-3 s-1 when the enzymeconcentration is 3.60 x 10-9 mol dm-3. Calculate koat and the catalytic efficiency η. Is the enzyme 'catalytica lly perfect'?
Ql- A carbohydrate (S) decomposes in the presence of an enzyme. The change of substrate concentration with initial reaction rate It's in the table below. Evaluate the value of Km &Vmax by employing the Langmuir plot. Concentration Cs Rate rp 0.0064 0.222 0.0068 0.296 0.0089 026 0.0092 0332 0.0099 0.4
Sucrose is hydrolyzed to glucose and fructose in a classic experiment in kinetics. The reaction is catalyzed by the enzyme invertase. Using the following data, determine, by Lineweaver-Burk method, whether the inhibition of this reaction by 2 M urea is competitive or noncompetitive Sucrose concentration (M) V, No I (arbitrary unit) V, With I (arbitrary unit) 0.0292 0.182 0.083 0.0584 0.265 0.119 0.0876 0.311 0.154 0.117 0.330 0.167 0.175 0.372 0.192
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?
Problems on enzyme reaction kinetics 1. Initial rates of enzyme-catalyzed reaction for various substrate concentrations are listed below: Rate Substrate concentration mol/(L min)x10 177 (mol/L) 0.0041 173 0.00095 0.00052 125 106 0.000103 80 0.000049 0.0000106 0.0000051 67 43 a) Evaluate Vmax and Km by a Lineweaver-Burk plot.
(i) For the following reaction catalysed by an enzyme E E +S ES k-1 E + P describe the meaning of the Steady State Assumption; define the reaction rate, V; outline the relationship between the reaction rate, V, and the molarity of the free substrate, [S], if the Steady State Assumption is valid; • outline the Lineweaver-Burk plot for the above reaction. (ii) Modify the above reaction for the cases of Competitive, Noncompetitive and Uncompetitive inhibitions. (ii) Outline the effects of the Competitive, Noncompetitive and Uncompetitive inhibitions on the Lineweaver-Burk plot.
The protein catalase catalyzes the reaction 2H,0,(aq) – 2 H,0O(0) + 0,(g) and has a Michaelis–Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s-1. The total enzyme concentration is 0.016 µM and the initial substrate concentration is 6.58 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax ) for this enzyme. Rmax mM-s- Calculate the initial rate, R (often written as Vo), of this reaction. R = mM-s-
Reaction Velocity (mm/sec) Ma no !! L [1 1 L IM 3M FO Substrate Concentration (M) 1. IN Which statement is true? KM AN ALM 4V The graph above displays the kinetic profiles of the same enzyme catalyzing two different substrates. The red curve displays the higher turnover number (kcat). The red curve displays higher affinity between substrate and enzyme. The blue curve displays competitive inhibition. The red curve displays higher cooperativity,

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