Question

) Compound competes with for binding to the active site of synthase. Explain how increasing the concentration of can reverse the inhibitory effect of Compound on the reaction catalyzed by synthase

Answer 1

Enzyme inhibition occurs when a molecule binds to an enzyme and reduces its activity.

How does this inhibition occur?

In the case of competitive inhibition, the inhibitor (Compound A) binds to the active site of the enzyme, preventing the substrate (S) from binding. As a result, the reaction catalyzed by the enzyme slows down or stops altogether.

Increasing the concentration of the substrate can reverse the inhibitory effect of Compound A because it outcompetes the inhibitor for binding to the active site. When the concentration of S is high enough, there is a greater chance that S will bind to the active site, displacing Compound A. As more S molecules bind to the active site, the rate of the reaction catalyzed by synthase increases.

This principle is illustrated by the following equation:

`([ES])/([E]) = (K_m )/([S])`

where:

[ES] = concentration of the enzyme-substrate complex

[E] = concentration of the enzyme

`K_m` = Michaelis constant, which is the concentration of substrate at which the reaction rate is half of its maximum

[S] = concentration of substrate

In conclusion, increasing the concentration of substrate can reverse the inhibitory effect of Compound A on the reaction catalyzed by synthase by outcompeting the inhibitor for binding to the active site.

Complete question:

Compound A competes with substrate S for binding to the active site of synthase. Explain how increasing the concentration of substrate S can reverse the inhibitory effect of Compound A on the reaction catalyzed by synthase.