molMalate dehydrogenase catalyzes the oxidation of malate to oxaloacetate with a standardGibbs free energy of AG° = +29.7*. What is the equilibrium constant (Keq) for thisreaction at 298 K and pH 7? Under physiological conditions at 310 K and pH 7, thisreaction is at equilibrium. In the mitochondrial matrix, the ratio NAD+/NADH is 8 andthe concentration of malate is 1.0 mM. What is the concentration of oxaloacetate? Malatedehydrogenase is also present in the cytoplasm where the ratio NAD+/NADH is 700 andmalate concentration is 1.0 mM. If this reaction is at equilibrium at 310 K and pH 7, whatis the cytosolic concentration of oxaloacetate?malate + NAD+ oxaloacetate + NADH + H+

Malate dehydrogenase (MDH) is a crucial enzyme in cellular metabolism, catalyzing the reversible…

Answered: mol Malate dehydrogenase catalyzes the…

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 46QAP: Glycolysis is the process by which glucose is metabolized to lactic acid according to the equation...

See similar textbooks

Similar questions

When the reaction below reaches equilibrium, does the equilibrium lie on the left or the right side? Briefly explain. ClO– + CH3CO2H ⇌ HClO + CH3CO2– When the terminal phosphate is cleaved from the adenosine triphosphate molecule, the products are adenosine diphosphate and inorganic phosphate, ATP + H2O ––> ADP + Pi, where Pi stands for the various forms of phosphate that exist at the pH of the particular solution. If the total concentration of Pi is 2.5 x 10–2M, what are the concentrations of the predominant forms of phosphate that exist at pH 7.4? Permanganate, MnO4–, can act as an oxidizing agent in both acidic and basic aqueous solutions. Balance each of the following reactions by the half–reaction method, showing all steps in the balancing process. MnO4– + Al ––> MnO2 + Al(OH)4– in aqueous base MnO4– + CH3COOH ––> Mn+2 + CO2 in aqueous acid
The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-
Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG" for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.45 mM [oxaloacetate] = 0.110 mM [NAD] = 450 mM [NADH] = 180 mM AG: -3.046 Incorrect 1 kJ.mol-¹
Based on the following information for phosphoglucoisomerase, calculate the equilbrium constant and round to the nearest tenths place. R = 8.3145 J/mol⋅K ΔG∘’ = -14.2 kJ/mol
The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?
GiventhatthechangeinGibbsfreeenergyforthehydrolysisofATPcorresponds to ∆rGm = −31 kJ mol-1 under the conditions prevailing in a typical cell, can the hydrolysis drive the formation of glutamine?
2. Experimental Determination of Keq' and AG If a 0.1 M solution of glucose 1-phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Glucose1-phosphate glucose6-phosphate 9.6 x 10-2 M 4.5 x 10-3 M Calculate Keg' and AG for this reaction.
When the following reaction reached equilibrium the concentration of glucose 1-phosphate is 34mM, and the concentration of glucose 6-phosphate is 190mM. At standard temperatures and pressure, calculate the Keq and the ΔGo' glucose 6-phosphate <---(phosphoglucoisomerase)---> glucose 1-phosphate Keq= ΔGo' =
3) Calculate the physiological AG for the reaction: Phosphocreatine + ADP - creatine + ATP at 25 °C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM, knowing that Phosphocreatine + H20 - creatine + Pi AG° = -43 kJ/mol and ATP + H20 ADP + Pi AG = -30.5 kJ/mol
Glycerol kinase catalyzes the phosphorylation of glycerol from ATP, yielding glycerol-3-phosphate and ADP. The standard state free energy for hydrolysis of glycerol-3- phosphate is -9.20 kj/mol and for the hydrolysis of ATP is-30.5 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the glycerol kinase reaction at 37 *C. AG kj/mol Keq Submit Answer Try Another Version 10 item attempts remaining
Part b
What is the standard free energy (∆G0’) for the reduction of coenzyme Q by NADH as carried out by Complex I (NADH-CoQ Reductase) of the electron transport pathway if E0’(NAD+/NADH) =-0.10 V and E0’ (CoQ/CoQH2) = +0.095 V. Answer Choices

SEE MORE QUESTIONS

Recommended textbooks for you

Chemistry: Principles and Reactions

Chemistry

ISBN:

9781305079373

Author:

William L. Masterton, Cecile N. Hurley

Publisher:

Cengage Learning

General Chemistry - Standalone book (MindTap Cour…

Chemistry

ISBN:

9781305580343

Author:

Steven D. Gammon, Ebbing, Darrell Ebbing, Steven D., Darrell; Gammon, Darrell Ebbing; Steven D. Gammon, Darrell D.; Gammon, Ebbing; Steven D. Gammon; Darrell

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305080485

Author:

John E. McMurry

Publisher:

Cengage Learning

Chemistry: Principles and Reactions

Chemistry

ISBN:

9781305079373

Author:

William L. Masterton, Cecile N. Hurley

Publisher:

Cengage Learning

General Chemistry - Standalone book (MindTap Cour…

Chemistry

ISBN:

9781305580343

Author:

Steven D. Gammon, Ebbing, Darrell Ebbing, Steven D., Darrell; Gammon, Darrell Ebbing; Steven D. Gammon, Darrell D.; Gammon, Ebbing; Steven D. Gammon; Darrell

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305080485

Author:

John E. McMurry

Publisher:

Cengage Learning

Introduction to General, Organic and Biochemistry

Chemistry

ISBN:

9781285869759

Author:

Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:

Cengage Learning

Chemistry for Today: General, Organic, and Bioche…

Chemistry

ISBN:

9781305960060

Author:

Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:

Cengage Learning

Introductory Chemistry For Today

Chemistry

ISBN:

9781285644561

Author:

Seager

Publisher:

Cengage

SEE MORE TEXTBOOKS