Plz help The MichaelisMenten equation models the hyperbolic

Plz help!

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 doubleheadarrow 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. Incorrect At least one statement is not matched to its correct condition. The rate of reaction is proportional to [ES]. At low S concentration, most of the enzyme is in the E_free form. As S concentration increases, more substrate becomes bound and the rate increases.

Solution

WHEN S<KM kinetics follow first order so rate is directly proportional to S

AT KM, V= V(MAX)/2 MEANS at km half of enzyme is occupied so AT S=KM E(free)=E(occupied) applies

When S>KM condition of enzyme saturation follows 0 order rate , so all sites would be occupied, reaction rate would be independant of s because no enzyme would be available

Here is a glitch i guess increasing E(TOTAL) should result in more free enzyme BUT IT WONT AFFECT Km( instead of decrease as shown in question) ...

Regarding 4th box E(s) is much lower than E(free) holds true at lower concentrations of substrate as substrate is less than enzyme ie s>>km Es will always be less than E(free) ....... and hence it applies to box 1 instead of (NOT TRUE FOR ANY OF THESE CONITIONS

It is very difficult to explain question of this sort, i tried my best to help, feel free to discuss and comment i will be glad if i can be of any more help .....

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Regarding topics in michael menton kinetics i guess the best way is to go for a video class on chegg and i can help u understand the core concepts of enzyme kinteics there.....

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