Km and Vmax dependence on enzyme concentration

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SUMMARY

The discussion centers on the relationship between Vmax and Km in enzyme kinetics, specifically under Michaelis-Menten kinetics. Vmax is directly proportional to enzyme concentration, expressed as Vmax = k2[E]. In contrast, Km, defined as the substrate concentration at which the reaction velocity is half of Vmax, remains independent of enzyme concentration. This independence arises because Km reflects the equilibrium constant for the formation of the enzyme-substrate complex (E + S <-> ES), which does not vary with substrate concentration as long as the reaction adheres to first-order kinetics.

PREREQUISITES
  • Understanding of Michaelis-Menten kinetics
  • Familiarity with enzyme-substrate interactions
  • Knowledge of equilibrium constants in biochemical reactions
  • Basic grasp of reaction order in kinetics
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  • Study the derivation of Michaelis-Menten kinetics in detail
  • Explore the concept of enzyme-substrate complex formation
  • Investigate the implications of first-order kinetics in biochemical reactions
  • Learn about the effects of varying enzyme concentrations on reaction rates
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This discussion is beneficial for biochemists, molecular biologists, and students studying enzyme kinetics, particularly those interested in understanding the dynamics of enzyme activity and substrate interactions.

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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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