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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Mitochondrial Mutations

A mitochondrion is a cellular organelle that serves as the site for cellular respiration and energy production (ATP or Adenosine Triphosphate). It is a double-membrane-bound organelle and is only present in eukaryotic cells.