New answers tagged

2

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 ...


2

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 ...


Top 50 recent answers are included