Is increasing the P; concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation?Yes. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right.No. The phosphate salts of divalent cations would be present in excess and precipitate out.No. The extra P; would give a negative AG", but would give a positive AG.Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction.

It makes sense to relate ATP hydrolysis and glucose phosphorylation by increasing the P…

Answered: Is increasing the P; concentration a…

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

See similar textbooks

Similar questions

Which of the following sequences represents the correct general sequence of oxidative fatty acid catabolism? (1) NAD+ dependent oxidation(2) FAD-dependent oxidation(3) thiolysis(4) hydration Please explain...thanks
. Avidin is a protein that binds extremely tightly to biotin. Therefore, it is a potent inhibitor of biotin-requiring enzyme reac- tions. Consider glucose biosynthesis from each of the following substrates and predict which of these pathways would be inhibited by avidin. (a) Lactate (b) Oxaloacetate (c) Malate (d) Fructose-6-phosphate (e) Phosphoenolpyruvate
Imagine a typical enzyme kinetic curve of [S] vs. V. The maximum [S] is about four times the Km. Lines are drawn at [S] = Km and V = Vmax. The asymptote is drawn at [S] = 0. 1. What effect does altering Km have on Vmax? Explain. 2. What effect does altering [E] have on Km? Vmax? Explain. 3. At what concentration of [S] is the initial velocity proportional to [E]? Explain.
In enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.
Draw out the complete pathway for the elongation of a glycogen molecule by two residues 9.) starting from sucrose. (You need to show how both the glucose and fructose are converted into glycogen.) Draw all the structures and name all of enzymes. You do not need to draw the structures of ATP, NAD*, CoA, etc., but do show them as reactants or products in the appropriate places. You do not need to show the mechanisms of the enzymes.
Show summary computation in a table Net ATP yield for complete oxidation of 1 mol of galactose to CO2 and H2O (using both Malate-Aspartate and Glycerol-3-Phosphate Shuttles)
Calculate glucose concentration. Na (sodium) and glucose secondary active transport. Na transport (which drive glucose import) G=R*T*In(Na in/ Na out)+Z*F*Y(psi symbol) Na in=14mM Na out=145MM Z=+1 F=96.5 KJ/V*mol Y(psi)=-0.05V What is the glucose in and out concentration? Please be very through when explaining this calculation. (I am stuck at why the energy sign changes from negative to positive when using the calculated energy from sodium to glucose)
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)?
The standard free energy change for ATP hydrolysis is -7.3kcal/mol. The free energy change under typical cellular conditions is about -12kcal/mol. Why is there a difference? O The hydrolysis of ATP must be more difficult in the cellular environment O There is more ATP and less ADP in the cell O The cellular environment is anaerobic so O2 levels are reduced O The enzymes involved in the reaction are trapped in organelles
Substrate level phosphorylation is the spontaneous transfer of phosphate from an organic substrate to ADP. These organic substrates have a [more/less/equivalent] negative free energy of hydrolysis than ATP. In glycolysis, 4 total ATP are produced in this way from a single molecule of glucose in [1/2/4] different enzymatic reactions/steps in the [investment/payoff] phase. please help with the ones in []
How does the allosteric enzyme kinetics different from M-M kinetics? Draw a graph to show allosteric enzyme kinetics (initial rate vs [S]. Show how the graph change in the presence of + effector and negative effector.
Phosphofructokinase-1 (PFK-1) catalyzes the transfer of a phosphoryl group from ATP to fructose 6-phosphate, Shown is a graph of the rate of PFK-1 vs. [ATP], Concisely explain the shape of the graph. 2 (ATP) (mmol l) PFK-1 reaction rate

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS