.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con-centration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy chargeof 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration ofADP divided by the total adenine nucleotide concentration:[ATP] + 1/2[ADP][ATP] + [ADP] + [AMP]

ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in…

Answered: .Intramitochondrial ATP concentrations…

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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2+ The activity of the Ca 2+ -ATPase is regulated reversibly under normal conditions to maintain homeostatic concentrations of Ca²- inside the sarcomere. However, in a rare genetic disorder, irreversible activation of the Ca 2+ -ATPase can occur. Assuming 37 °C, pH = 7.4, and the steadystate concentrations for ATP, ADP Pi, and Ca2+ (out) given in part (a), calculate the minimum [Ca2+] inside a sarcomere that has irreversibly activated Ca 2+ -ATPase (i.e., the Ca2+-ATPase activity is always “on”). Express your answer to two significant figures and include the appropriate units.
Calculate the ATP yield for the full catabolism of a phospholipid containing ethanolamine, C18:3 Δ9, 12, 15 and oleic acid. Include any ATP “expenses” or “income”. This will be a complex problem—neatly show your work and justify your choices.
1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?
Lysozyme is a catalytic enzyme that cleaves NAG-NAM units in the bacte- rial cell wall, and is found in external secretions of the body. Why does this
From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?
Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.
Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.
In class, I mentioned that fructose is metabolized differently in the liver compared to glucose. Refer to the figure shown below to calculate the number ofATPs you would expect from the metabolism of fructose in the liver. Show your work! Fructokinase Fructose Fructose-1-P АТР ADP Aldolase B Dihydroxy- acetone phosphate Glyceraldehyde АТР Triose kinase Triose phosphate isomerase ADP 4 - Glyceraldehyde-3-P Glycolysis Руruvate Acetyl-CoA Fatty acids and triglycerides
V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.
mutations in adenylate kinase have led to a hyperactive enzyme that ultimately ends up elevating adp levels in a cell.calculate Ec given the following atypical adenylate concentrations for the cell containing atp: .o5 mM adp 12.2mM and amp 80micromole
Describe the categories of enzyme control: (image provided) Allosteric control with example Covalent modification with example
When 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a solution containing its substrate at a concentration 100 times the Km, it catalyzes the conversion of 65 micromoles of substrate into product in 3 minutes. What is the enzyme's turnover number (in units of min-1)?

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