### Enzyme Kinetics Analysis of Aldolase**Problem Statement:**You are studying the kinetic behavior of the enzyme aldolase, which converts the substrate, fructose 1,6-bisphosphate (FBP), into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (G3P). You collect the following data by measuring the rate of G3P formation:#### Data Table| \([FBP]\) (mM) | Rate (µmol/min) | \(\frac{1}{[FBP]}\) | \(\frac{1}{\text{rate}}\) ||----------------|-----------------|--------------------|------------------|| 0.25 | 8.3 | 4 | 0.12 || 0.50 | 13.5 | 2 | 0.074 || 1.00 | 19.4 | 1 | 0.052 || 2.50 | 26.5 | 0.4 | 0.038 || 5.00 | 30.2 | 0.2 | 0.033 |**Instructions:**a) **Table Completion:** - Calculate and fill in \(\frac{1}{[FBP]}\) and \(\frac{1}{\text{rate}}\) columns based on the given data.b) **Graph Plotting:** - On graph paper, create a double reciprocal plot (Lineweaver-Burk plot) using the values in the table. - Ensure to label the axes clearly.c) **Line Drawing:** - With a ruler, draw the best straight line through the plotted points.d) **Calculations:** - Use the line to calculate \(K_m\) and \(V_{max}\), the Michaelis-Menten constants that describe these data.**Graph Description:**- The graph is a Lineweaver-Burk plot, which is a double reciprocal plot used to analyze enzyme kinetics.- The x-axis represents \(\frac{1}{[FBP]}\) and the y-axis represents \(\frac{1}{\text{rate}}\).- The plot is linear, and the slope of the line gives \(\frac{K_m}{V

For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…

Answered: 1. You are studying the kinetic…

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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2. The overall result of CH,OH + 2 NAD+ + 2 NADH glycolysis can be summarized by the equation on the right in which HO the glucose origins of the carbon atoms in pyruvate are color coded. Show by writing the reactions catalyzed by aldolase and triose phosphate isomerase and num- bering the carbons why this is the fate of glucose carbon atoms in pyruvate. Indicate numbering of carbons in Glucose-6-Pi, Fructose-1,6-BisPi, enzyme products, and pyruvate. HO + 2 Pi 2 + 2 ATP > OH + 2 ADP (CH3 + 2 H20 Glucose Pyruvate
1. Cyanide, oligomycin, and 2,4-dinitrophenol are all inhibitors of oxidative phosphorylation in mitochon- dria. Provide an explanation to the following conditions regarding these potent inhibitors. (a) Explain why adding cyanide to an active in vitro suspension of mitochondria blocks ATP synthesis. What happens to the rate of ATP synthesis when 2,4-dinitrophenol is added to this mitochon- drial suspension after it was treated with cyanide? (b) Explain why the rate of oxygen consumption decreases in an in vitro suspension of mito- chondria when oligomycin is added. What happens to the rate of oxygen consumption in this oligomycin- inhibited system after adding 2,4-dinitrophenol? Explain.
The data below show the inhibition of rat liver alcohol dehydrogenase (ADH) by tetramethylene sulfoxide, a drug that is used to treat methanol poisoning. What form of ADH does tetramethylene sulfoxide bind to? 8 A [1] = 0.6 mM 0.4 mM ミ。 0.2 mM 2 0.5 1.0 1.5 2.0 2.5 1/(ethanol), mM -1 O Only to the free enzyme, E. O Only to the enzyme-substrate complex, ES. O To both E and ES, but with higher affinity for E. O To a serine residue at the enzyme active site. O To both E and ES, with equal affinity.
21. Based upon the following reactions, what would be the AG" for the formation of ATP from phosphoenolpyruvate and ADP? ATP → ADP + Pi phosphoenolpyruvate pyruvate + Pi AG" = -31.5 kJ/mol AG"=-62.2 kJ/mol
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
10. The first reaction in glycolysis is the phosphorylation of glucose: Pi + Glucose → Glucose-6-phosphate This is a thermodynamically unfavorable process with AGº = +13.8 kJ/mol. In a liver cell at 37 °C the concentration of both phosphate and glucose are normally maintained at about 5 mM each. The equilibrium concentration of glucose-6-phosphate according to the above data is: A. 1.18 x107 B. 8.50 x 104 C. 4.25 x 105 D. 2.21 x 10s E. 1.38 x 108 F. 3.02 X 103 G. 6.75 x 10-6 H. 4.08 x 10 I. 9.15 x106
1. The phosphorylation of glucose with HPO42- forms glucose 1-phosphate and water and requires 5.0kcal/mol of energy. a. Write the equation for this reaction. b. This unfavorable reaction can be driven by the hydrolysis of ATP to ADP. Write the equation for the coupled reaction. c. Calculate the energy change for coupled reaction
5. During prolonged fasting, amino acids derived from muscle proteins and connective tissue become the main substrate for gluconcogenesis. How does glutamate enter the gluconeogenesis? For answer: a) write a reaction of the glutamate conversion into a-ketoglutarate, name the enzyme, indicate the encrgy effect of the reaction; b) draw a diagram for the a-ketoglutarate conversion to oxaloacetate and consequent including of OAA to gluconcogenesis, specify the reactions associated with ATP consumption; c) name the hormones that accelerate gluconeogenesis during fasting and regulatory enzymes of the process; and describe the mechanism of signal transduction by these hormones.
6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
8
7. Representative values of Vm and ApH for the inner mitochondrial membrane and the thylakoid membrane at 25°C are provided in the table. Vm Арн 1.0 pmf Inner mitochondrial 0.166 V 0.2251 membrane Thylakoid membrane O,1483 0.03 V B) What is the value of AG for the thermodynamically feasible (“downhill") movement of 1 mole of H across the inner mitochondrial membrane?
11. Chambers and coworkers have reported [NAD*] and [NADH] concentrations in yeast mitochondria as 20 mM and 0.3 mM, respectively. Consider the Malate Dehydrogenase reaction below: Malate + NAD* → Oxaloacetate + NADH + H* AG° = +29.7 kJ/mol If Malate concentration in yeast mitochondria is 0.4 mM what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 37°C? А. 7.14 х 105 В. 2.04 х 104 С. 8.17 х 106 D. 5.45 x 108 Е. 2.63 х 107 F. 4.69 x 108 G. 4.90 X107 Н. 3.13 х 106 I. 5.05 х 106

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