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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explain in quantitative terms the circumstances under which the following reaction can porceed; L-malate + NAD+ (forward arrow) oxaloacetate + NADH + H+ delta G' standard = +29.7 KJ/mol
The standard reduction potential for (NAD+/NADH) is -0.320 V and the standard reduction potential for (pyruvate/lactate) is -0.185 V. Which of the following statements are TRUE? i Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation... SHOW MORE ✓ a b с d e f The standard free energy change (AGO) for the Lactic acid dehydrogenase reaction is -26 kJ/mol. The Keq for the reaction is 36800. If [pyruvate] = 0.05 mM and [Lactate] =2.9 mM and AG for the Lactate dehydrogenase = -15 kJ/mole in erythrocytes the [NAD+]/[NADH] ratio under these conditions is 1.48. The standard reduction potential indicates the electrons will flow from Lactate to NAD+. AEO' for the reaction = -0.135 V The standard reduction potential indicates the electrons will flow from NADH to Pyruvate.
A mutant version of DADH can use NADP+ as a cofactor for isopropanol oxidation. Velocity data was collected from reactions at a series of NADP+ concentrations. The following trendline was obtained for a Lineweaver-Burk plot of the data: y = 0.00007x + 0.0014 Note that the NADP+ substrate concentrations are in mM and the reaction velocity was measured in nmol/min. Calculate the Km and Vmax for DADH with this substrate. Show your work.
The glutamate dehydrogenase (GDH) catalyses the following reaction: *H₂N- H CH₂ CH₂ COO™ acide glutamique COO™ Time (min) A340 + NAD+ + H₂O The answer: GDH 2 1 1.760 1.718 [ammonium sulphate] = 0.33 M [NADH] = 0.205 mg.mL-¹ = 2.9.10-4 M [a-ketoglutarate] = 0.07 M [Protein] = 0.05 mg.mL-¹ COO™ CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. 5 3 4 1.675 1.635 1.595 !- Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. CH₂ The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M-¹.cm-¹ COO acide x-cétoglutarique O + NH4+ + NADH + H* 6 1.550…
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).
a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
Calculate the ΔG for Malate dehydrogenase reaction of CAC if the concentration of oxaloacetate is 1x 10-8 M, malate is 0.2 mM, NAD+ is 10 mM and NADH is 0.1 mM in rat liver mitochondria. ΔGo’ for this reaction is 30 kJ/mole. Please write the units of the final answer and the formula you are using to solve. R = 0.008314kJ/K*mol, T = 298K
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 11/12102 + 2H* + 2e¯ → H₂0 NAD + H* + 2e → NADH O-1.136 volts 0.496 volts +1.136 volts -0.496 volts EU (volts) – 0.320
The enzyme lactate dehydrogenase catalyzes the reversible reaction lactate (CH3 CHOHCOO )+NAD* рyruvate (CH3 COCOO) + NADH + H+ Given the standard reduction potentials CH3 СОСОО + 2H+ + 2е CH3 CHОНСО" E°'= -0. 185 V NADŤ + H+ + 2e- → NADH = -0. 320 V E°' would you expect the reaction to be spontaneous in the forward or reverse direction under biochemical standard state conditions? How could you change the reaction conditions to force the reaction to be spontaneous in the opposite direction? Please explain your answer.

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