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Chapter 18: Problem 8

If \(^{32}\) P-labeled inorganic phosphate were introduced to erythrocytes undergoing glycolysis, would you expect to detect \(^{32} \mathrm{P}\) in glycolytic intermediates? If so, describe the relevant reactions and the \(^{32} \mathrm{P}\) incorporation you would observe.

Short Answer

Expert verified
Yes, if \(^{32}P\) were introduced, it would be detected in the glycolytic intermediates. The labeled \(^{32}P\) would be incorporated into 1,6-bisphosphate in step 6, 3-phosphoglycerate in step 7, and phosphoenolpyruvate in step 10 of glycolysis.

Step by step solution

01

Understanding Glycolysis

Glycolysis is a metabolic pathway involving several enzymatic reactions. It breaks down one glucose molecule into two molecules of pyruvate, releasing energy in the form of ATPs. During this process, specific steps involve transfer or consumption of inorganic phosphate (P).
02

Identifying Phosphate transfer reactions in Glycolysis

Analyzing glycolysis, there are three reactions where inorganic phosphate is incorporated or transferred and would therefore possibly contain the \(^{32} \mathrm{P}\) tag: The first transfer occurs in the 6th step of glycolysis, in which glucose 1-phosphate is converted into 1,6-bisphosphate using an inorganic phosphate. The other two transfers occur in the 7th and 10th steps. In the 7th step, 1,6-bisphosphate is converted into 3-phosphoglycerate and 2-phosphoglycerate is converted into phosphoenolpyruvate in the 10th step.
03

Describing \(^{32} \mathrm{P}\) Incorporation

If \(^{32} \mathrm{P}\) were introduced to erythrocytes undergoing glycolysis, it could be incorporated into the phosphates and used during these glycolytic phosphorylation processes. Thus, it is reasonable to expect that \(^{32} \mathrm{P}\) would be identifiable in the glycolytic intermediate products - 1,6-bisphosphate,3-phosphoglycerate and phosphoenolpyruvate.

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Most popular questions from this chapter

Fructose bisphosphate aldolase in animal muscle is a class I aldolase, which forms a Schiff base intermediate between substrate (for example, fructose- 1,6 -bisphosphate or dihydroxyacetone phosphate and a lysine at the active site (see Figure 18.12 ). The chemical evidence for this intermediate comes from studies with aldolase and the reducing agent sodium borohydride, \(\mathrm{NaBH}_{4}\). Incubation of the enzyme with dihydroxyacetone phosphate and \(\mathrm{NaBH}_{4}\) inactivates the enzyme. Interestingly, no inactivation is observed if \(\mathrm{NaBH}_{4}\) is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.

(Integrates with Chapter \(3 .)\) The standard free energy change \(\left(\Delta G^{\circ \prime}\right)\) for hydrolysis of fructose- 1,6 -bisphosphate (FBP) to fructose6-phosphate (F-6-P) and \(\mathrm{P}_{\mathrm{i}}\) is \(-16.7 \mathrm{kJ} / \mathrm{mol}\) \\[ \mathrm{FBP}+\mathrm{H}_{2} \mathrm{O} \longrightarrow \text { fructose- } 6-\mathrm{P}+\mathrm{P}_{\mathrm{i}} \\] The standard free energy change \(\left(\Delta G^{\circ \prime}\right)\) for ATP hydrolysis is \(-30.5 \mathrm{kJ} / \mathrm{mol}\) \\[ \mathrm{ATP}+\mathrm{H}_{2} \mathrm{O} \longrightarrow \mathrm{ADP}+\mathrm{P}_{\mathrm{i}} \\] a. What is the standard free energy change for the phosphofructokinase reaction: \\[ \text { ATP + fructose- } 6 \text { -P } \longrightarrow \mathrm{ADP}+\mathrm{FBP} \\] b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and [ADP] are maintained constant at \(4 \mathrm{m}\) Mand \(1.6 \mathrm{m} M\), respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?

(Integrates with Chapter \(3 .)\) Triose phosphate isomerase catalyzes the conversion of dihydroxyacetone-P to glyceraldehyde-3-P. The standard free energy change, \(\Delta G^{\circ}\) ', for this reaction is \(+7.6 \mathrm{kJ} / \mathrm{mol}\). However, the observed free energy change \((\Delta G)\) for this reaction in erythrocytes is \(+2.4 \mathrm{kJ} / \mathrm{mol}\) a. Calculate the ratio of [dihydroxyacetone-P]/ [glyceraldehyde-3-P] in erythrocytes from \(\Delta G\) b. If [dihydroxyacetone-P] \(=0.2 \mathrm{m} M\), what is [glyceraldehyde-3-P]?

(Integrates with Chapters \(4 \text { and } 14 .)\) How might iodoacetic acid affect the glyceraldehyde- -phosphate dehydrogenase reaction in glycolysis? Justify your answer.

Regarding phosphofructokinase, which of the following statements is true: a. Low ATP stimulates the enzyme, but fructose- 2,6 -bisphosphate inhibits. b. High ATP stimulates the enzyme, but fructose- 2,6 -bisphosphate inhibits. c. High ATP stimulates the enzyme, but fructose- 2,6 -bisphosphate inhibits. d. The enzyme is more active at low ATP than at high, and fructose- 2,6 -bisphosphate activates the enzyme. e. ATP and fructose- 2,6 -bisphosphate both inhibit the enzyme.
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