Researchers isolated a yeast phosphofructokinase (PFK) mutant in which a serine at the fructose-2,6-bisphosphate binding site was replaced with an aspartate residue. The amino acid substitution completely abolished the binding of fructose-2,6-bisphosphate to PFK. There was a dramatic decline in glucose consumption and ethanol production in the mutant compared to control yeast. What does the decline of glucose consumption and ethanol production in the yeast show about the function of fructose-2,6-bisphosphate in glycolysis

Biology: The Dynamic Science (MindTap Course List)
4th Edition
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Chapter15: From Dna To Protein
Section15.1: The Connection Between Dna, Rna, And Protein
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Researchers isolated a yeast phosphofructokinase (PFK) mutant in which a serine at the fructose-2,6-bisphosphate binding site was replaced with an aspartate residue. The amino acid substitution completely abolished the binding of fructose-2,6-bisphosphate to PFK. There was a dramatic decline in glucose consumption and ethanol production in the mutant compared to control yeast. What does the decline of glucose consumption and ethanol production in the yeast show about the function of fructose-2,6-bisphosphate in glycolysis?

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