Chapter 18: Problem 2
Determine the anticipated location in pyruvate of labeled carbons if glucose molecules labeled (in separate experiments) with \(^{14} \mathrm{C}\) at each position of the carbon skeleton proceed through the glycolytic pathway
Chapter 18: Problem 2
Determine the anticipated location in pyruvate of labeled carbons if glucose molecules labeled (in separate experiments) with \(^{14} \mathrm{C}\) at each position of the carbon skeleton proceed through the glycolytic pathway
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Get started for freeIn an erythrocyte undergoing glycolysis, what would be the effect of a sudden increase in the concentration of a. ATP? b. AMP? c. fructose- 1,6 -bisphosphate? d. fructose- 2,6 -bisphosphate? e. citrate? f. glucose- 6 -phosphate?
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.
Based on your reading of this chapter, what would you expect to be the most immediate effect on glycolysis if the steady-state concentration of glucose- 6 -P were \(8.3 \mathrm{m}\) M instead of \(0.083 \mathrm{mM}\) ?
Discuss the cycling of NADH and NAD \(^{+}\) in glycolysis and the related fermentation reactions.
(Integrates with Chapter 3 .) Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate \(+\mathrm{H}_{2} \mathrm{O}\). The standard free energy change, \(\Delta G^{\circ},\) for this reaction is \(+1.8 \mathrm{kJ} / \mathrm{mol}\). If the concentration of 2 -phosphoglycerate is \(0.045 \mathrm{m} M\) and the concentration of phosphoenolpyruvate is \(0.034 \mathrm{m} M\), what is \(\Delta G\), the free energy change for the enolase reaction, under these conditions?
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