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Biology, 19.04.2021 15:40 mckenzeebrown1578
Researchers isolated a yeast phosphofructokinase mutant in which a serine at the fructose-2,6-bisphosphate (F26BP) binding site was replaced with an aspartate residue. The amino acid substitution completely abolished the binding of F26BP to PFK. There was a dramatic decline in glucose consumption and ethanol production in the mutant compared to control yeast.
Required:
a. Propose a hypothesis that explains why the mutant PFK cannot bind F26BP.
b. What does the decline of glucose consumption and ethanol production in the yeast reveal about the role of F26BP in glycolysis?
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Researchers isolated a yeast phosphofructokinase mutant in which a serine at the fructose-2,6-bispho...
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