1.So then why do you say that your enzyme is stimulated by ssDNA at the beginning of your text? What are the evidences? you could for instance have the same Vmax but while measurring product appearance, your enzyme could reach steady state faster? coudl you explain better?Also not sure what do you mean Vmax and Kcat, the kcat is just Vm:[E]0

2.there are many ways enzyme can be regulated. Already what you can say by now is that the Km is lower plus DNA meaning that the affinity is better, of course this result in a higher catalytic efficiency (Vm:Km) that will be higher then.

hope it will help a bit in your reasoning

Because Vmax is unchanged, the stimulation of activity resulting from decreasing the Km(ATP) from 2.45 µM to 1.25 µM would only be observed at ATP concentrations lower than saturation. Since typical ATP concentrations in cells is in the mM range, this slight effect on the ATP Km would not result in any measurable effect on the activity of the enzyme in its native environment.

@Brigitte Gontero . By performing ATPase assay using radioactive ATP, we could see that the product formation is 3-4 fold higher in the presence of DNA than in its absence, when we titrate Protein. And yes we should compare either Vmax or Kcat. Thank you very much for your suggestions. I will consider the fact while doing experiment that whether protein is achieving steady state faster or not.

@Adam B Shapiro thank you very much. Yes, it is helpful. i shall use concentration of ATP far less than the saturating concentrations in the experiment.