Km and Vmax dependence on enzyme concentration

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Vmax is directly related to enzyme concentration, as expressed in the equation Vmax = k2[E]. However, Km, which represents the substrate concentration at which the reaction velocity is half of Vmax, does not depend on enzyme concentration. This is because Km is defined as the equilibrium constant for the formation of the enzyme-substrate complex (E + S <-> ES) and remains constant regardless of the concentration of the enzyme. The confusion arises from the relationship between Vmax and Km; while increasing Vmax indicates a higher maximum reaction rate, it does not imply that Km will also increase, as Km is independent of substrate concentration under the assumptions of first-order kinetics and a steady-state condition where the concentration of the enzyme-substrate complex is nearly constant. For further clarification, a thorough derivation of Michaelis-Menten kinetics can be found on Wikipedia.
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We know that Vmax depends on enzyme concentration since Vmax = k2[E]

However, what I have trouble grasp is that why Km does not depend on enzyme concentration if Km is the substrate concentration where V = 1/2 Vmax. If you increase Vmax, shouldn't Km increase as well since it is dependent on it?

I asked my biochem prof today and he gave some explanation about substrate concentration which I didn't catch. I am hoping someone can clarify it here. thanks!
 
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If K_M = then
v_0 = v_{max}\frac{<s>}{K_M+<s>}=v_{max}\frac{<s>}{2<s>}=\frac{v_{max}}{2}</s></s></s></s>

Note though, that this doesn't mean K_M is dependent on . K_M is defined as a measure of the equilibrium constant for E + S <-> ES. Which is not dependent on any concentration, as long as the reaction is first order, which Michaelis-Menten kinetics assumes. (it also assumes a steady-state where [ES] is near-constant)

I see http://en.wikipedia.org/wiki/Michaelis–Menten_kinetics" has a thorough derivation of Michaelis-Menten kinetics, btw.
 
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