A biologist wants to increase the rate of his chemical reaction but has a limited amount of enzyme. He continues to increases the substrate concentration instead. Eventually, the reaction rate levels off, and he can't get it to go any faster. What prevented the rate from increasing further?

Question

anonymous · Answer

The solution ran out of enzyme

The substrate concentration reached Vmax

The products of the reaction inhibited the enzyme

The solution ran out of reactants

anonymous · Answer

I has reached the equilibrium point.

shrutipande9 · Answer

see for an enzymatic reaction...the substrate binds to the enzyme and den the substrate is converted to product. so for instance if u have 100 molecules of enzyme then at a time only 100 substrate molecules get converted to product..so even if u keep on increasing the substrate conc after a certain point it does not affect the rate of reaction...

aaronq · Answer

This is what the $v$ vs [S] plot looks like
|dw:1399211062737:dw|

After you've added enough S to saturate the system the michealis menten equation changes from  $v=\dfrac{V_{max}[S]}{[S]+K_m}$ to  $v=V_{max}$, a zeroth order reaction.

There could be several reasons why the rate plateaus, like the products can inhibit the enzyme because they, too, bind the active site. But i think the answer they're looking for is that [S] reached the $V_{max}$ concentration.

anonymous · Answer

Thanks a bunch