While doing research on an enzyme one of my graphs was sigmoidal and I need to find km and vmax however I can't find a good article to explain how to do this since the graph doesn't follow the Michaelis-Menten model.
Km is for michaelian enzymes, the equivalent for allosteric enzymes is called K0.5. Vm is determined experimentally by measuring v0 at saturating S0 (Vm is much more accessible for allosteric enzymes than for purely michaelian enzymes because the transition is full and generally occurs at managable substrate concentrations). For graphical determination of K0.5 you need to plot ln(v0/(Vm-v0))=f(lnS0), the slope will be nH (Hill number) and x axis intercept will be ln(K0.5).