Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energychange for this reaction at energy change for this reaction at 37.0 °C (310 K). AG" for the reaction is +29.7 kJ/mol. Assumethat the reaction occurs at pH 7.[malate] = 1.27 mM[oxaloacetate] = 0.210 mM[NAD+] = 320 mM[NADH] = 130 mMAG:-48.5kJ.mol-¹

Malate dehydrogenase catalyses the reversible conversion of malate (MAL) to oxaloacetate (OAA),…

Answered: Consider the malate dehydrogenase…

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 the following enzymes (3-6) predict how the conditions will most likely affect the enzymes activity with one of the following and provide a 1 sentence explanation: a. increase activity b. decrease activity c. not likely to alter activity 3) alpha-ketoglutarate dehydrogenase complex binding to AMP when [AMP] is high. 4) phosphohexose isomerase binding NADH when [NADH] is high 5) phosphofructose-1 binding NAD+ when [NAD+] is high 6) pyruvate dehydrogenase complex binding to ATP when [ATP] is high
Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
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
Under standard conditions, will the following reactions proceed spontaneously as written? (1) Fumarate + NADH + H+ (2) succinate + NAD+ Cyto a (Fe²+) + cyto b (Fe³+) = cyto a (Fe³+) + cyto 6 (Fe²+) b
Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/mol
All dehydrogenases of glycolysis and the TCA cycle use NAD* (E° for NAD*/NADH is -0.32V) as electron acceptor except succinate dehydrogenase (which uses FAD (E° for FAD/FADH2 is 0.05V). Based on AG° = -NFEº, show and state (1-2 sentences) why is FAD a more appropriate electron acceptor than NAD* in the dehydrogenation of succinate (consider the E° values of %3D Uptake in Na+ Vmax Uptake in absence of Na+ Vmax substrate K: (mM) Kt (mM) L-leucine 420 0.24 23 0.2 D-Leucine 310 4.7 5 4.7 L-valine 225 0.31 19 0.31 fumarate/succinate (E° = 0.031), NAD*/NADH, and the succinate dehydrogenase FAD/FADH2).
(b) number of moles of ATP produced under aerobic glycolysis whereby pyruvate enters the mitochondrion for oxidative decarboxylation to generate acetyl-CoA that enters the citric acid cycle. Write the reac- tions for each step using words. They need not be balanced with respect to charge, protons released or consumed, and stoichiometry. Consider 2.5 ATP/NADH oxidized and 1.5 ATP/FADH2 oxidized. Enzymes need not be named. Compare the number of moles of ATP that are produced under anaerobic glycolysis to the Of the reactions producing ATP in the mitochondrion listed in part (b) above, which are not (c) influenced by the proton gradient across the inner mitochondrial membrane?
The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
Write a balanced equation for the complete metabolic oxidation of each of the following. Include O, ADP, and P; as reactants and ATP, CO, and H;0 as products. (a) Stearic acid (b) Oleic acid (c) Palmitic acid (d) Linoleic acid
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

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