The glutamate dehydrogenase (GDH) catalyses the following reaction:*H₂N-HCH₂CH₂COO™acide glutamiqueCOO™Time (min)A340+ NAD+ + H₂OThe answer:GDH211.760 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-¹COO™CH₂The activity of GDH is monitored in the sense of the formation of glutamate using thefollowing conditions:0.2 mL of 5 M ammonium sulphate2.4 mL of buffer at pH 80.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹)0.2 mL of 1 M a-ketoglutarate solutionWarm mixture at 25 °C for 5 minAdd 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start thereaction.5341.675 1.635 1.595!- Calculate ammonium sulphate, NADH,concentrations in the reaction medium at t = 0.CH₂The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minutefor 10 min. Results are given in the table below:Data ENADH at 340 nm = 6220 M-¹.cm-¹COOacide x-cétoglutariqueO+ NH4+ + NADH + H*61.550781091.510 1.489 1.476 1.451a-ketoglutarate and proteins

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Answered: The glutamate dehydrogenase (GDH)…

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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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.
The Eo values for the NAD/NADH and Glyceraldehyde-3-phosphate/1,3- Bisphosphoglycerate conjugate redox pairs are -0.32 V and -0.19 V, respectively. Beginning with 1 M concentrations of each reactant and product at pH 7 and 25 C, which statement is TRUE? Glyceraldehyde-3-phosphate would become oxidized; NAD would become reduced. No reaction would occur because all reactants and products are already at their standard concentrations. Glyceraldehyde-3-phosphate would become oxidized; NADH2 would be unchanged because it is a cofactor. Glyceraldehyde-3-phosphate and 1,3-Bisphosphoglycerate would become oxidized; NAD and NADH would become reduced. 1,3-Bisphosphoglycerate would become reduced; NADH would become oxidized.
The glutamate dehydrogenase (GDH) catalyses the following reaction: *H3N- C H - CH₂ - CH₂ COO™ acide glutamique -COO + NAD+ + H₂O Time (min) A340 GDH COO™ с 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ The answer: -1 - Vo 1.1.107 M.s-¹ - EA in 0.1 mL of GDH = 0.33 nkat 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 protein to start the reaction. COO CO acide a-cétoglutarique 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 M¹.cm¹ -1 + NH4+ NADH + H+ 6 1.550 7 8 10 9 1.510 1.489 1.476 1.451 Calculate the initial rate Vo of the reaction in M.s¹. - Calculate the enzyme activity of the volume of…
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 glutamate dehydrogenase (GDH) catalyses the following reaction: H +H₂N- -C -COO CH₂ CH₂ COO™ acide glutamique + NAD + H₂O GDH Time (min) A340 COO™ c=o CH₂ 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ COO + NH4+ NADH + H+ acide a-cétoglutarique 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. 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 M¹.cm7 6 7 8 9 10 1.550 1.510 1.489 1.476 1.451 Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. proteins - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. -…
Consider the two half-reactions below and their standard reduction potentials. NAD+ + H+ + 2e → NADH Elo= -0.32 V a-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V (a) What is AE" for the spontaneous redox reaction that is, the reaction that actually occurs under standard biochemical conditions (pH 7)? (b) Which of the following statements are correct under standard biochemical conditions? i. The concentration of H+ is 1.0 M. ii. The reaction NAD+ + Isocitrate → NADH + H+ + a-Ketoglutarate + CO₂ is favor- able. iii. NAD+ accepts electrons from isocitrate. iv. The NAD → NADH reaction actually occurs in reverse. The a-ketoglutarate → isocitrate reaction occurs as written. (c) Calculate AG" for the reaction in (a). (pH 7, 25°C, pressure, 1 atm.) (d) Suppose that the actual conditions are T = 25°C, pH = 7, CO₂ = 1 atm, [a-Ketoglutarate] 10 mM, [NAD+] = 2.5 mM, and [NADH] = 0.5 mM. PAR = 2 mM, [Isocitrate] DE What is the value of AG under those conditions? (Hints: pH 7 is already…
Given the following information, calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pH 7.0: [NAD+]/[NADH] = 8, [α-ketoglutarate] = 0.1 mM, and [isocitrate] = 0.02 mM. Assume standard conditions for CO2 (ΔG°′ is given in Table). Is this reaction a likely site for metabolic control?
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
A new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?
a) The following reaction which is catalyzed by aldolase: Fructose-,6-bisphosphate (FBP) + Glyceraldehyde 3-phosphate (GAP) + Dihydroxyacetone phosphate (DHAP) AG for this reaction is 22.8 kJ mol'. In the cell at 37°C, AG for this reaction is -5.9 kJ mol". Determine the ratio [GAP][DHAP]/[FBP]
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?
The half-reactions involved in the lactate dehydrogenase (LDH) reaction and their standard reduction potentials are (see attached)). Calculate ΔG at pH 7.0 for the LDH-catalyzed reduction of pyruvate under the following conditions: (a) [lactate]/[pyruvate] = 1 and [NAD+]/[NADH] = 1. (b) [lactate]/[pyruvate] = 160 and [NAD+]/[NADH] = 160. (c) [lactate]/[pyruvate] = 1000 and [NAD+]/[NADH] = 1000. (d) Discuss the eff ect of the concentration ratios in Parts a–c on the direction of the reaction.

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