The conversion of glucose to glucose 6-phosphate is an endergonic reaction (eql below). The second equation below is an exergonicreaction that can occur in all cells. Considering this information, how can the reaction in equation 3 proceed?EQ1: Glucose + Pj--> glucose 6-phosphateEQ2: ATP + H20 --> ADP + PjEQ3: Glucose + ATP --> glucose 6-phosphate + ADPSelect one:a. The energy required to make Eq3 spontaneous is provided by the enzyme catalyzing the reactionb. The energy released from equation 1 is more than the energy consumed in equation 2 making the overall reaction AG negativeand the reaction spontaneous.c. The energy released from equation 2 is more than the energy consumed in equation 1 making the overall reaction AG positiveand the reaction spontaneous.d. The energy released from equation 2 is more than the energy consumed in equation 1 making the overall reaction AG negativeand the reaction spontaneous.e. The energy released from equation 1 is more than the energy consumed in equation 2 making the overall reaction AG positiveand the reaction spontaneous.

Free energy or Gibbs energy is the portion of the total energy available to carry out work. The…

Answered: The conversion of glucose to glucose…

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

Starting with glucose, there are five steps in the EMP/TCA metabolic pathways that produce NADH (which is converted to ATP or energy). Use class notes, Shuler, Kargi and DeLisa book, or the internet. 1. A. Draw the chemical structures of the reactant(s) and product(s); as well as a balanced chemical reaction for the step in the TCA (Krebs) cycle where isocitrate is converted to a-ketoglutarate (step 3 in the class notes). (You don't need to draw the structures of coenzyme A (COA), NAD* or NADH.) B. What enzymes catalyze steps 3 and 5 in the Kreb's cycle from the class notes? C. Would you categorize step 8 in the TCA cycle where malate is converted to oxaloacetate as an oxidation or reduction of malate? D. Considering that some energy is spent transporting acetyl-CoA to mitochondria, how much net energy (in kcal) is produced by converting 15 mol of glucose to CO₂ in the glycolysis & Krebs cycle pathways? E. How many kcals of energy from oxidizing 15 mol of glucose to CO₂ (your answer to…
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
Using the data in this table, what is the AG° (in KJ/mol) for the reduction of FAD by water?
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.
How many net ATP are produced from the complete oxidation of one molecule of 1,3-bisphosphoglycerate (1,3 BPG) in a neuron?
A solution of [U 14C] glucose-1-phosphate (specific activity = 16,000 cpm/mmole) was incubated with glycogen and glycogen phosphorylase, an enzyme which adds glucose units on to glycogen. Radioactivity was incorporated into the glycogen primer at a rate = 2550 cpm/min. The rate of the enzymatic reaction in units of mmole glucose incorporated per minute is: (a) 0.016 mmol/min (b) 0.57 mmol/min (c) 0.16 mmol/min (d) 5.7 mmol/min
The products of a pathway, or the products of specific reactions in the pathway, will often inhibit upstream regulatory enzymes in that pathway. That makes sense - if the products of a pathway are abundant, then the pathway can be shut off to save energy or divert molecules into other pathways. We can use a similar rule of thumb to predict whether a pathway will be active in different biological states. For example, the liver stores glucose (in the form of glycogen), and will release glucose into the bloodstream when blood sugar levels drop. This glucose can come from the synthesis of glucose or breakdown of stored glycogen. This is important for maintaining blood sugar levels. What would you predict is the relationship between blood sugar levels and glycogen phosphorylase enzyme activity? A positive relationship (when blood sugar levels are high, glycogen phosphorylase activity is also high). A negative relationship (when blood sugar levels are high, glycogen phosphorylase activity…
Table 9.2 shows that DGo’ for the aldolase reaction is large, and positive, yet the reaction proceeds in the forward direction. Using the metabolite concentrations in table 9.3, calculate the actual DG in the cell for the reaction to show that it is consistent with the value reported in table 9.2. Explain in words the strategy the cell uses to keep glycolysis moving in the forward direction (1-2 sentences).
The table contains data about how different ASFV mutants affect enzyme activity-- for example the D29A mutant, where the D at position 29 was mutated to an A. Select three mutants at random, and for each mutant explain how that mutation could affect intermolecular force interactions (an example: hydrogen bonding could be disrupted by this mutation because…
A mutation has occurred that results in phosphofructokinase not being able to bind ATP in its allosteric site. What impact will this mutation have on the production of ATP in the cell? Select one: a. If no ATP can bind to the allosteric site, then phosphofructokinase will not be able to add the phosphate to fructose-6-phosphate to make fructose-1,6-bisphosphate and glycolysis will not work. So no pyruvate, not cellular respiration. b. If ATP cannot bind to the allosteric site, phosphofructokinase will not be activated to make more ATP by substrate-level phosphorylation. c. No impact on the production but will not be able to effectively shut off over production of ATP with feedback inhibition.
The following two reactions are coupled in the last step of glycolysis (catalyzed by the enzyme pyruvate kinase). РЕР + Н.О € Руr + Pi ADP + Pi → ATP + H2O AG° = -14.8 kcal/mol AG° = +7.3 kcal/mol D) The steady-state concentrations of ATP, ADP, and pyruvate in human erythrocytes are 2.24 mM, 0.25 mM, and 0.051 mM, respectively. What would be the concentration of PEP in these cells if the coupled reaction was at equilibrium?
The following Michaelis-Menten plot shows the response of phosphofructokinase-1 (PFK-1), an enzyme in the glycolytic pathway, to the presence of ATP and AMP. Based on the data below, which of the following statements apply? Select all that apply. No inhibitors (low (ATP)) 1 mM ATP + 0.1 mM AMP 1 mM ATP 1.0 2.0 (Fructose-6-phosphate) mM Fig. : Regulation of PFK activity AMP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate а. O b. AMP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate ATP is an allosteric modifier that reduces the binding of the substrate fructose 6-phosphate O c. O d. ATP is an allosteric modifier that enhances the binding of the substrate fructose 6-phosphate Phosphofructokinase activity

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