The MichaelisMenten equation models the hyperbolic relations

The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial reaction rate (V_0) for an enzyme catalyzed, single substrate reaction: E + S ES rightarrow E + P. The model can be more readily understood when comparing three conditions: [S] K_m. Match each statement with the condition that it describes.

Solution

Km is the Michelis-Mentons constant, that represents the Substrate concentration, at which the enzyme velosity is half of its maximum velosity.

In other words Km = Disociation / Association. So Km is less, E & S affinity is more and Velocity of the enzymatic reaction is also more

[S] <<Km =====> Almost all active sites are empty,

[S] = Km ======> [Efree] is equal to [ES], This condition rarely occurs for most in vivi enzymes

[S] >> Km =======> [E free] is about equal to [Etotal], [ES] is much higher than [E-Free]

NOT TRUE FOR ANY OF THESE CONDITIONS: Increasing [E-Total] will lower Km