A) Effect of Enzymes on Reactions Which of the following effects (a-g) would increase the rate of an enzyme catalyzing the simple reaction as shown below. k SP where K = [P]/[S] k₁ (a) Decreased Keq (b) Increased k (c) Increased Keq (d) Increased G (e) Decreased G (f) More negative G (g) Increased k B) The Turnover Number of Carbonic Anhydrase Carbonic anhydrase of erythrocytes (Mr 30,000) has one of the highest turnover numbers we know of. It catalyzes the reversible hydration of CO₂: HO+CO, HCO, This is an important process in the transport of CO, from the tissues to the lungs. If 10.0 g of pure carbonic anhydrase catalyzes the hydration of 0.30 g of CO, in 1 min at 37 °C at V, what is the turnover number (k) of carbonic anhydrase (in units of min')? (hint [E] and [S] are expressed in moles for this problem.) max

A) Effect of Enzymes on Reactions Which of the following effects (a-g) would increase the rate of an enzyme catalyzing the simple reaction as shown below. k SP where K = [P]/[S] k₁ (a) Decreased Keq (b) Increased k (c) Increased Keq (d) Increased G (e) Decreased G (f) More negative G (g) Increased k B) The Turnover Number of Carbonic Anhydrase Carbonic anhydrase of erythrocytes (Mr 30,000) has one of the highest turnover numbers we know of. It catalyzes the reversible hydration of CO₂: HO+CO, HCO, This is an important process in the transport of CO, from the tissues to the lungs. If 10.0 g of pure carbonic anhydrase catalyzes the hydration of 0.30 g of CO, in 1 min at 37 °C at V, what is the turnover number (k) of carbonic anhydrase (in units of min')? (hint [E] and [S] are expressed in moles for this problem.) max

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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For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
The formation of maltose, a disaccharide, from two glucose molecules, is not energetically favorable. However, if this reaction is coupled with the hydrolysis of ATP, the reaction occurs more favorably. Maltose + H2O = 2 Glucose , ΔG'o = -15.5 KJ/mol or -3.7 kcal/mol a. Determine if the coupled reaction will occur spontaneously at standard state through calculating the Gibbs Free Energy of Reaction. b. Calculate the equilibrium constant for each individual reaction, and for the coupled reaction (using free energy of reaction). Show that the equilibrium constant for the coupled reaction equals the equilibrium constants for the individual reactions multiplied together. c. If the reaction medium contains the following chemical species at their given concentrations (298 K and 1.0 atm, pH = 7.0), will the reaction proceed in the forward or the reverse direction? [Maltose] = [Glucose] = 10.0 mM; [ATP] = 5.0 mM; [ADP] = [Pi] = 20 mM
Which of the following statements about a plot of V0 vs. [S] for an enzyme that follows Michaelis-Menten kinetics is false? a. As [S] increases, the initial velocity of reaction V0 also increases. b. At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at Km. c. Km is the [S] at which V0 = 1/2 Vmax. d. The shape of the curve is a hyperbola. e. The y-axis is a rate term with units of μm/min.
You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!
The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.
An enzyme catalyzes a reaction at a velocity of 20 μmol/min when the concentration of substrate (S)is 0.01 M. The Km for this substrate is 1 × 10-5 M. Assuming that Michaelis-Menten kinetics arefollowed, what will the reaction velocity be when the concentration of S is 1 ×10-6 M?
You have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product. Based on the data table and your initial…
a. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.
If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.