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Application of the Michaelis-Menten equation generally assumes steady state concentration of the enzymatic complex intermediate. Then $K_M$ allows two interpretations$^1$: an apparent dissociation constant describing the equilibrium $$\ce{ES<=>E +S}\tag{1}$$ where $E$ and $S$ are the concentrations of enzyme and substrate, respectively the ...
The Michaelis–Menten kinetics model formula is: $$V= \frac{(d¦P¦)}{dt} = \frac{(Vmax)¦S¦}{Km + ¦S¦}$$ Reaction rate V is the rate of formation of product, ¦P¦ is the concentration of product and the ¦S¦ the concentration of a substrate S. In a saturated regime V = Vmax and this occours only if: $$\frac{¦S¦}{Km + ¦S¦} \approx 1$$ This is nearly equal to ...