You are studying a biochemical pathway that requires ATP as an energy source. To your dismay, the reactions soon stop, partly because the ATP is rapidly used up and partly because an excess of ADP builds up and inhibits the enzymes involved. You are about to give up when the following table from a biochemistry textbook catches your eye creatine+ ATP → creatine phosphate + ADP; AG (+)3 kcal / mol ATP + H₂O → ADP + phosphate; AG = (-)7.3 kcal / mol Glucose-6-phosphate + H₂O → glucose + phosphate; AG= (-)3.3 kcal/mol What is about these equations that provides a solution to your problem? If you add enough creatine, ATP will be regenerated If you add enough ADP, ATP will be regenerated If you supply creatine phosphate, ADP will be depleted and more ATP produced. This will allow your reactions to continue Supplying glucose-6-phosphate will provide enough free phosphate to regenerate ATP

You are studying a biochemical pathway that requires ATP as an energy source. To your dismay, the reactions soon stop, partly because the ATP is rapidly used up and partly because an excess of ADP builds up and inhibits the enzymes involved. You are about to give up when the following table from a biochemistry textbook catches your eye creatine+ ATP → creatine phosphate + ADP; AG (+)3 kcal / mol ATP + H₂O → ADP + phosphate; AG = (-)7.3 kcal / mol Glucose-6-phosphate + H₂O → glucose + phosphate; AG= (-)3.3 kcal/mol What is about these equations that provides a solution to your problem? If you add enough creatine, ATP will be regenerated If you add enough ADP, ATP will be regenerated If you supply creatine phosphate, ADP will be depleted and more ATP produced. This will allow your reactions to continue Supplying glucose-6-phosphate will provide enough free phosphate to regenerate ATP

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter2: Cell Physiology

Section: Chapter Questions

Problem 2SQE

See similar textbooks

Similar questions

You are studying a biochemical pathway that requires ATP as an energy source. To your dismay, the reactions soon stop, partly because the ATP is rapidly used up and partly because an excess of ADP builds up and inhibits the enzymes involved. You are about to give up when the following table from a biochemistry textbook catches your eye. A. ذن فه B. Substrates C. Creatine + ATP ATP + H₂O Pyrophosphate + H₂O Glucose-6-phosphate + H₂O Enzyme A Enzyme B Enzyme C Enzyme D Products Creatine-phosphate + ADP Which of the following reagents is/are most likely to revitalize your reaction? a vast excess of ATP glucose 6-phosphate and enzyme D creatine phosphate and enzyme A D. pyrophosphate ADP + Phosphate 2 Phosphate Glucose + Phosphate AG (kJ/mol) +3 -7.3 -7.0 -3.3
2 3 4 5 B Type here to search 6 7 8 9 10 O O 3 4 5 6 7 8 9 10 pH Level The 11 A researcher investigates the effect of eight different pH levels on the reactions catalyzed by the enzyme catalase. All other factors are held constant. Based on the following graph, what can you conclude about the relationship between the catalase and pH? Reaction Rate by pH Level O T 12 13 optimal (highest) pH level of catalase is 6.5. As the pH level increases, the reaction rate increases. As the pH level decreases, the reaction rate increases. There is no relationship between the pH level and the reaction rate. 14 W 15 16 DELL 17 18 19 20 21 22 → G 23 24 25 3:57 PM 9/15/2022 D D
A 75 kg person doing light work requires about 3000 kcal of food energy perday, 40% of which is actually used by the body’s cells. (The other 60% is lostas heat and in waste products.) Before being used by the cells, effectively allof this energy is stored in ATP, which is then cleaved into ADP and PO3−2 , with the release of 12.5 kcal per mole of ATP.(a) How many moles of ATP are turned over per day in this fashion? Whatmass of ATP does this correspond to? (The molecular weight of ATP is507 g/mol.)(b) The body actually contains approximately 5 g ATP. Estimate the averagerecycle time for an ATP molecule. You see that it is much more efficientto reuse ADP rather than to synthesize it de novo (from scratch).
The biosynthesis of vitamin D₂ is a two-step reaction, requiring two types of concerted pericyclic reactions. Draw in the arrows for each step and identify the structure of precalciferol. If an electrocyclic reaction is required, identify if it occurs through a conrotatory or disrotatory reaction. HO H H ergosterol hv precalciferol Cast HO ergocalciferol
Two experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)
The standard free energy of hydrolysis of inorganic polyphosphate (polyP) is about −20 kJ/mol for each Pi released. We calculated in Worked Example 13–2 that, in a cell, it takes about 50 kJ/mol of energy to synthesize ATPfrom ADP and Pi. Is it feasible for a cell to use polyphosphate to synthesize ATP from ADP? Explain your answer.
Which of the compounds shown below exhibit a high negative free energy of hydrolysis equal to or larger than the free energy of hydrolysis for the phosphoanhydride of ATP? (Choose all that apply) В Α HPΗ Ho HO HO H2N-CH-C CH2 H2N-CH-C CH2 CH2 H2N-CH-Ö CH2 C CH2 D E O A O B O E O=p-00 O=p-00 O=-00 O=0-00 O=L-00
Assume a cell undergoes the Aerobic Respiration option of catabolism. Calculatethe number of ATP molecules that it could theoretically generate if it starts with each of thefollowing molecules. 4. a) A dipeptide containing a 4-carbon amino acid and a 5-carbon amino acid b)A 20-unit polypeptide (each unit = a 2-carbon amino acid) c)one glycerol molecule
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG°) of ATP = -31 kJ/mol; RT = 2,58 kJ/mol) Select one: O a. -28 kJ/mol O b. -33 kJ/mol OC. -19 kJ/mol O d. -42 kJ/mol
As a result of an experiment following measurements were obtained from a cell: ATP concentration of 0.5 mM, ADP concentration of 0.1 mM, inorganic phosphate (Pi) concentration of 2 mM. Under these conditions calculate the actual free energy (AG) of the reaction of hydrolysis of ATP to ADP and Pi. (The standard energy (AG") of ATP = -31 kl/mol; RT = 2.58 kJ/mol) Select one: a. -28 kJ/mol b. -33 kJ/mol C. -42 kJ/mol d. -19 kJ/mol
Table 2: Effect of pH on Enzyme Activity pH Absorbance 2 0.05 4 0.35 6 0.8 8 0.5 10 0.4 12 0.1 Use the above data table to complete the following questions: a) Plot the data “pH Vs Abs” using “connect the data point type of graph”. Label the graph with dependent and independent variables where they should be. Provide a title for the graph. b) Over what pH range does catechol oxidase catalyze catechol to benoquinone? c) Explain why the graph has a bell-shaped curve.
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase