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. Why can't the mutant PFK bind with fructose-2,6-bisphosphate?
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. Why can't the mutant PFK bind with fructose-2,6-bisphosphate?
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
Problem 1SB
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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. Why can't the mutant PFK bind with fructose-2,6-bisphosphate?
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