Chemistry, 23.03.2020 23:46 zay179

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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Answer from: sophiav9780

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

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

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

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

_____________________________________________|____________

[ES] is much | | Almost all active

lower than | | sites are filled

$[E_{free}]$ | |

Explanation:

Generally the combined enzyme [ES] is mathematically represented as

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

for Michaelis-Menten equation

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

Considering the statement [S] < < K_M

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

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

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

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

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

Considering the second statement

[S] = K_M

So this means that equation one would now become

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

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

Considering the Third Statement

[S] K_M

In this case the K_M in the denominator of equation 1 would be neglected and the equation becomes

$[ES] = \frac{[E_{total}] [S]}{[S]} = [E_{total}]$

This means that almost all the sites are occupied with substrate

The rate of this reaction is mathematically defined as

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

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

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

$v = \frac{V_{max}[S]}{[S]} = V_{max}$

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 $[E_{total}]$ will lower K_M

This is because K_M does not depend on enzyme concentration it is a property of a enzyme

Enzyme‑catalyzed, single‑substrate reaction E + S − ⇀ ↽ − ES ⟶ E + P . The model can be more readily

Answer from: Quest

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Answer from: Quest

Outermost (valence) electrons

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Enzyme‑catalyzed, single‑substrate reaction E + S − ⇀ ↽ − ES ⟶ E + P . The model can be more readily...

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