3. Show that the inverse of equation 29-78 in the textbook gives the Lineweaver-BurkEquation.The hydration of CO2 is catalyzed by the enzyme carbonic anhydrase. For a total enzymeconcentration of 2.32 x 10-⁹M, the following data were obtained.[CO2]o (M) v (M/s)0.001252.78 x 10-50.002505.00 x 10-50.005008.33 x 10-50.02000 1.66 x 10-4Plot these according to the Burke-Lineweaver Equation and determine the values of Km, theMichaelis constant, and k2, the rate constant for product formation from the enzyme-substratecomplex from the slope and intercept of the plotted data.

The Michaelis-Menten (MM) equation is the general equation used in most enzyme kinetic studies. The…

Answered: 3. Show that the inverse of equation…

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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Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/mol
Pharmaceuticals When a medicine is administered orally, the concentration of the drug in the patient's circulation after t minutes is given by C(t) = 0.06t – 0.00021, where Osls 240 and the concentration is measured in mg/L. When does the highest serum concentration occur, and what is that maximum serum concentration?
A monoprotic weak acid, HA, dissociates in water according to the reaction HA(aq) = H+ (aq) + A¯(aq) The equilibrium concentrations of the reactants and products are [HA] = 0.220 M, [H+] = 3.00 × 10−4 M, and [A¯] = 3.00 × 10−4 M. Calculate the value of pKa for the acid HA. pKa =
The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)
Use the Michaelis-Menten equation to complete the enzyme kinetic data set, whenKm is known to have a value of 1 mmol L−1 [S] (mmol L−1) Vo (μmol L−1 min−1) 0.5 50 1.0 2.0 3.0 10.0
You just made a 1.5M permanganate solution. What concentration is your potassium permanganate solution in percent? "K: 39.10 g/mole" "Mn: 54.94 g/mole" "O: 16 g/mole" "MW of KMnO4 is 158.04 g/mole" O a. 0.24% Ob. 20.1% O c. 15.8% O d. 23.7% O e. 2%
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
Compound A is the substrate for two enzymes, El and E2, their reaction rates, r1 and r2,Determine the Km and rmax for both enzymes, with respect to the concentration of A. Which set of data is more likely to be for El and which for E2, and why? Concentration of 0.2 0.6 1.2 3 4 5 6 8 12 15 A (mM) Reaction rate (r.) (mmol/L'min) 3.33 4.29 4.62 4.76 4.84 4.88 4.9 4.92 4.94 4.95 4.96 4.97 Reaction rate (r,) (mmol/L*min) 0.09 0.23 0.38 0.5 0.6 0.67 0.71 0.75 0.8 0.82 0.86 0.80
[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
An enzyme with concentration of 3.0 uM is added to a flask containing 125 uM of substrate. You know the Km is equal to 0.054 mM, and has a Vmax of 1.4 uM/s. What is the observed velocity? O 0.98 uM/s 0.074 uM/s O 5.2 um/s 1.4 uM/s

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