Final answer:
A mutant enzyme with increased substrate affinity would have a decreased Michaelis-Menten constant (KM), which would be represented on a graph as a shift to the left.
Step-by-step explanation:
If an experiment uses a mutant enzyme that increases the enzyme's affinity for its substrate, we would expect a change in the Michaelis-Menten constant (KM). The KM value is inversely related to the enzyme's affinity for its substrate; hence a higher affinity corresponds to a lower KM value.
Considering that the mutant enzyme binds its substrate more tightly, the KM would decrease. This means that in the graph comparing the wild-type enzyme to the mutant enzyme, the KM for the mutant enzyme would move to the left (decrease).