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In this video, I discuss the Michaelis-Menton Model for Enzyme Kinetics.
For a non-allosteric enzyme, reaction velocity plotted vs substrate concentration results in a hyperbolic graph. As substrate concentration increases, reaction velocity increases, at least until a certain point, where beyond a certain concentration, the reaction velocity remains the same; this the reaction’s maximum velocity or Vmax. At lower substrate concentrations, first order kinetics are observed, but at higher substrate concentrations, because of the Vmax plateau, 0th order kinetics are observed, due to the enzyme being saturated.
The hyperbolic graph has a hyperbolic equation associated with it, relating reaction velocity to Vmax, substrate concentration [S], and Km (the Michaelis-Menton constant). The Km is a combination of rate constants from the steady state equation (shown in the video), and it is effectively a measure of affinity between the enzyme and its substrate. A higher Km indicates a lower affinity, while a lower Km indicates a higher affinity. Km is NOT Vmax/2. Km happens to be equal to the substrate concentration when the reaction running at Vmax/2.
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