Intramitochondrial ATP concentrations are about 5 mM, and phos-phate concentration is about 10 mM. If ADP is five times moreabundant than AMP, calculate the molar concentrations of ADP andAMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at37 °C under these conditions. The energy charge is the concentra-tion of ATP plus half the concentration of ADP divided by the totaladenine nucleotide concentration:[ATP] + 1/2[ADP][ATP] + [ADP] + [AMP]

ATP (Adenosine triphosphate) is the energy stored in the body which is produces as the result of…

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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The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function ofsubstrate concentration in the following table: (a) What kind of inhibition (competitive, uncompetitive, or mixed) isinvolved?(b) Determine Vmax and KM in the absence and presence of inhibitor.
The drug troglitazone was used to treat diabetes but was withdrawn from the market when patientswho took the drug suffered from severe side effects. The data below show the activity of an enzymein the steroid biosynthetic pathway in the presence and absence of 10 µM troglitazone.[S] (µM) v0 (pmol min-1)Create a plot of 1/v0 vs. 1/[S]. Calculate KM and vmax in presence and absence of inhibitor. Whattype of inhibitor is troglitazone? Clearly support your answer.
Below is a plot of Vo vs. [S] for a specific allosteric enzyme under different conditions. Which of the following best describes the graph? 4 (S] O Adding a positive modulator to #2 would result in curve 3. Curve 1 represents maximum inhibition. Line 4 is valid exclusively for curves 1 and 2. Adding a positive modulator to #1 would result in curve 2. O Curve 3 represents the effect of a negative modulator added to curve 2.
For the mitochondrial membrane described in pic, how many protons must be transported to provide enough free energy for the synthesis of 1 mol of ATP (assuming standard biochemical conditions)?
Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
A particular enzyme has a ΔΔG‡ of -22.1 kJ mol-1 at 37.0 °C. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8
In a major metabolic pathway involving the monosaccharide glucose, one of the reactions involve the conversion of glucose to glucose-6-phosphate summarized below together with accompanying free energy change: glucose + phosphate = glucose-6-phosphate + H,0 AG = 13.8 kJ · mol-1 (Reaction 1) In cells, the production of G6P (Reaction 1 above) is coupled to a reaction that involves the hydrolysis of ATP to ADP (shown below, Reaction 2) which makes the overall reaction much more favorable to the production of glucose-6-phosphate. ATP + H,O = ADP + phosphate (Reaction 2) Why do you think coupling the production of glucose-6-phosphate to the hydrolysis of ATP makes the overall reaction spontaneous? What can you say about the free energy change accompanying the hydrolysis of ATP (Reaction 2)?
Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:

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