Question

IN MICHAELIS MENTEN GRAPH, HOW WOULD YOU INCREASE VELOCITY BEYOND Vmax?

Answer 1

In the following solution of Michaelis Menten equation in Enzyme Kinetics we find that the reaction takes place between a Substrate and an Enzyme (which is also a Limiting Reagent). The reaction stops when Enzyme (Limiting Reagent) is completely consumed in the reaction.

So, what do we get from here? Ans. Maximum concentration of Enzyme-substrate complex [ES]max solely depends on the concentration of the limiting reagent (i.e Enzyme). This Enzyme-substrate complex forms the final product leaving Enzyme out, by a slow rate (say k2). This slow rate determines the rate of overall reaction and therefore it is the Rate Determining Step (R.D.S).

Now, the Rate (v) is directly proportional to the concentration of Enzyme-substrate complex, and therefore v​​​​​​max will be directly proportional to the maximum concentration of Enzyme-substrate complex. And this maximum Enzyme-substrate complex concentration depends solely on Enzyme concentration. Therefore, we can increase the value of maximum rate (v​​​​​max) when we increase the amount of Enzyme we take in the beginning of the reaction.

The solved Michealis Menten equation is given below: