enzyme‑catalyzed, single‑substrate reaction E + S − ⇀ ↽ − ES ⟶ E + P . The model can be more readily understood when comparing three conditions: [ S ] << K m , [ S ] = K m , and [ S ] >> K m . Match each statement with the condition that it describes. Note that "rate" refers to initial velocity V 0 where steady state conditions are assumed. [ E total ] refers to the total enzyme concentration and [ E free ] refers to the concentration of free enzyme.

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Complete Question

The complete question is shown on the first uploaded image

Answer:

[S]<<KM             |   [S]=KM                  |  [S]>>KM                     | Not true

____________  |   Half of the active  | Reaction rate is         | Increasing

[tex][E_{free}][/tex] is about   |    sites are filled of  |    independent of      |  [tex][E_{Total}][/tex] will                                            

 equal to [tex][E_{total}][/tex]. |                                 |   [S]                             | lower KM

_____________________________________________|____________

[ES] is much       |                                 | Almost all active

 lower than         |                                 | sites are filled

[tex][E_{free}][/tex]                  |                                 |

Explanation:

Generally the combined enzyme[tex][ES][/tex] is mathematically represented as

                   [tex][ES] = \frac{[E_{total}][S]}{K_M + [S]}----(1)[/tex]

for Michaelis-Menten equation

Where [tex][S][/tex] is the substrate concentration and [tex]K_M[/tex] is the Michaelis constant

Considering the statement [tex][S] < < K_M[/tex]

  Looking at the equation [tex][S][/tex] is denominator so it can be ignored(it is far too small compared to [tex]K_M[/tex])  hence the above equation becomes

               [tex][ES] = \frac{[E_{total}][S]}{K_M}[/tex]

Since [tex][S][/tex] is less than [tex]K_M[/tex] it means that [tex]\frac{[S]}{K_M} < < 1[/tex]

so it means that [tex][ES] < < [E_{total}][/tex]

  What this means is that the  number of combined enzymes[tex][ES][/tex] i.e the number of occupied site is very small compared to the the total sites [tex][E_{total}][/tex]  i.e the total enzymes concentration which means that the free sites [[tex]E_{free}][/tex]  i.e the concentration of free enzymes is almost equal to [tex][E_{total}][/tex]

Considering the second statement

      [tex][S] = K_M[/tex]

So  this means that equation one would now become

           [tex][ES] = \frac{[E_{total}][S]}{2[S]} = \frac{[E_{total}]}{2}[/tex]

So this means that half of the active sites that is the total enzyme concentration are filled with S

Considering the Third Statement

      [tex][S] >>K_M[/tex]

In this case the [tex]K_M[/tex] in the denominator of equation 1 would be neglected and the equation becomes

       [tex][ES] = \frac{[E_{total}] [S]}{[S]} = [E_{total}][/tex]

This means that almost all the sites are occupied with substrate

 The rate of this reaction is mathematically defined as

             [tex]v =\frac{V_{max}[S]}{K_M [S]}[/tex]

Where v is the rate of the reaction(also know as the velocity of the reaction at a given time t) and [tex]V_{max}[/tex]  is he maximum velocity of the reaction

In this case also the [tex]K_M[/tex] at the denominator would be neglected as a result of the statement hence the equation becomes

                [tex]v = \frac{V_{max}[S]}{[S]} = V_{max}[/tex]

So it means that the reaction does not depend on the concentration of substrate [S]

For the final statement(Not True ) it would match with condition that states that increasing [tex][E_{total}][/tex] will lower [tex]K_M[/tex]

This is because [tex]K_M[/tex] does not depend on enzyme concentration it is a property of a enzyme

             

       

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