Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might take place. Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the intracellular concentration of P,. The increase in P, concentration would drive the unfavorable phosphorylation of glucose by P. Is increasing the P concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? No. The phosphate salts of divalent cations would be present in excess and precipitate out. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. Yes. Increasing the concentration of P, would decrease K'e and shift equilibrium to the right. No. The extra P, would give a negative AG, but would give a positive AG. In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP and glucose, forming a glucose-ATP-enzyme…arrow_forwardSaccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Two moles of glyceraldehyde-3-phosphatearrow_forwardam. 206.arrow_forward
- 24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…arrow_forward23. An important step in glycolysis is the formation of ATP and pyruvate from phosphoenol-pyruvate (PEP) and ADP. PEP ADP pyruvate+ATP The equilibrium constant (Keq) for this reaction is approximately 2.5x10°. Calculate standard free energy change (AG°') for this reaction. Show your work. onege b. Is the reaction exergonic or endergonic at standard conditions? If, at equilibrium, the concentrations of ADP and ATP are 0.2 mM and 2.0 mM, respectively, what is the equilibrium concentration ratio of [pyruvate] to [PEP]? Show your work. с.arrow_forward4. The reaction shown below is part of the glycolytic pathway. The standard free energy change for this reaction is +0.4 kcal'mol. Glucose-6-phosphate (G6P) > Fructose-6-phosphate (F6P) A) What is K,' for this reaction at 25°C?arrow_forward
- 7. Flow of carbon atoms. What is the fate of the radioac- tive label when each of the following compounds is added to a cell extract containing the enzymes and cofac- tors of the glycolytic pathway, the citric acid cycle, and the pyruvate dehydrogenase complex? (The ¹4C label is printed in red.) (a) (c) H3C H3C O C. O C. COO COO- (b) (d) H3C H₂C O C. O C. (e) Glucose 6-phosphate labeled at C-1. COO™ S-COAarrow_forwardThe following structure is ATP synthase. Which of the following statements is NOT true for the ATP synthase? B b2 6 a В a Y E H+ α C10 B ATP ADP + Pi N side 800000 P sidearrow_forward6arrow_forward
- draw 3 allosteric enzyme curves for glycogen synthesis in the presence of high AMP, high NADH, and no regulators on 1 graph.arrow_forward+ Explain why a strain of yeast with a defect in the enzyme alcohol dehydrogenase can grow well under aerobic conditions, but not under anaerobic conditions. The yeast strain grows well when aerobic because acetaldehyde is quickly converted to lactate. The yeast strain uses CO₂ to generate NAD+ when aerobic, but GAPDH needs NADH when anaerobic. The yeast strain grows equally well under aerobic and anaerobic, but polyphenol is lethal to this strain. The yeast strain cannot oxidize NADH to generate NAD+ for the GAPDH reaction when anaerobic. The yeast strain needs to generate ethanol in order to stimulate the PFK- 1 reaction when anaerobic.arrow_forward3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certain enzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chest muscles used for flying) of pigeon and pheasant are listed below. Vmax (umol substrate/min/g tissue) Enzyme Pigeon Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase 18.0 120.0 143.0 24.0 100.0 15.0 0.07 0.01 b. Compare oxygen consumption in the two birds.arrow_forward
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