The kinetics data shown in this graph are from the enzyme lactate dehydrognase, which catalyzes the redox reaction lactate + NAD* <-> pyruvate + NADH.Calculate the Km and Vmax values with correct units0.040.031/vo(min uM-) 0.02Recall:0.01Vo = Vmax[S]/(Km + [S])1/vo = (K/Vmax)(1/[S]) + 1/Vmax-0.02-0.010.010.020.030.040.050.060.071/[NAD*] (µM)

The graph that is peesnted is LB plot or Line weaverburk plot.This is a double reciprocal plot where…

Answered: The kinetics data shown in this graph…

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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82.16
Write out the full redox reaction that happens when both of these reactions are added to the same reaction where there is 1M concentrations of each reactant and products, pH7, and temeprature is 290K. Identify which compounds will be reduced and which compounds will be oxidized. redox reaction 1: Pyruvate¯ + 2H+ + 2e¯ → lactate¯ E'o(V) = -0.185 redox reaction 2: NAD+ + H+ + 2e¯ → NADH E'o(V) = -0.320
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
Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
Consider an enzyme that follows standard Michaelis-Menten kinetics and has the following kinetic constants: %3| k2 = 1.5 x 10? s1 Еo 3D 1 х 104 М = 1 x 104 M a. What is the value of the maximum rate VM? b. Prepare a hand-drawn quantitative plot on graph paper (not a simple sketch nor an EXCEL-generated graph) of the enzymatic reaction rate versus substrate concentration (like Fig 3-3) using the kinetic parameters given above. Be sure to label the axes and include numeric values on the axes. C. Based upon your hand drawn saturation plot, at what substrate concentration is the enzymatic reaction rate 75% of Vm?
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
1) Define metabolism and describe the importance of metabolism to life. 2) Calculate the change in free energy (∆G ) for the below reaction and answer the two follow up questions: Gfinal state = 3.4 kcal/ mol and Ginitial state = 10.7 kcal/ mol Recall: ∆G = Gfinal state – Ginitial state a. Is this a spontaneous or non-spontaneous reaction? Explain. b. Is there energy released from this reaction which can be used to do work? Explain. 2) List four conditions which impact an enzymes rate of activity. Explain.
can you explain what is happening in the attached graph? Figure 3: Lineweaver-Burke plot of alkaline phosphatase activity without inhibitor
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanine
Find the net potential
2.3

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