How The Concentration Of Enzyme And Substrate Affect The Rate Of Enzyme Action?

Enzyme concentration
Usually a very small amount of enzyme can consume a large amount of substrate. The rate of reaction depends directly on the amount of enzyme present at a specific time at unlimited substrate concentration. If two folds increase the amount of enzyme the reaction rate is doubled.

By increasing the enzyme molecules an increase is the number of active sites takes place.
At higher concentration of the enzyme the inhibitors will fall short. More active sites will convert the substrate molecules into products, in the given period of time. After a certain limiting concentration, the rate of reaction will no longer depend upon this increase.

Substrate concentration
At low concentration of substrate the reaction rate is directly proportional to the substrate available.If the enzyme concentration is kept constant and the amount of substrate is increased, a point is reached when a further increase in the substrate does not increase the rate of the reaction any more. This is because at high substrate level all the active sites of the enzyme are saturated with substrate. After this, the rate of enzyme reaction becomes steady and addition of the substrate will not have the positive effect.

1) Effect of enzyme concentration on the speed of enzymatic reaction From the relationship between the Mimen formula and the relationship between enzyme concentration and enzymatic reaction rate, it can be seen that the enzymatic reaction rate is proportional to the concentration of the enzyme molecule. When the molecular concentration of the substrate is sufficient, the more enzyme molecules, the faster the substrate is converted. But in fact, when the enzyme concentration is high, this relationship is not maintained and the curve tends to be flat. According to the analysis, this may be due to the high concentration of substrate entrainment with many inhibitors. 2) Effect of substrate concentration on enzymatic reaction rate In the biochemical reaction, if the concentration of the enzyme is constant and the initial concentration of the substrate is low, the enzymatic reaction rate is proportional to the substrate concentration, that is, the substrate Increase in concentration. When all the enzymes are combined with the substrate to form an intermediate product, the intermediate product concentration does not increase even if the substrate concentration is increased, and the enzymatic reaction rate does not increase. It can also be concluded that the enzymatic reaction rate is proportional to the initial concentration of the enzyme at the same substrate concentration. The initial concentration of the enzyme is large, and the rate of enzymatic reaction is large. Topoisomerase In the actual measurement, even if the enzyme concentration is sufficiently high, the enzymatic reaction rate does not increase or even be inhibited as the substrate concentration increases. The reason is that the high concentration of the substrate reduces the effective concentration of water, reduces the molecular diffusivity, and reduces the rate of enzymatic reaction. Excess substrate accumulates on the enzyme molecule, producing an inactive intermediate that does not release the enzyme molecule, which in turn reduces the rate of reaction.

If the enzyme molecules constant then by increasing the substrate ,the reaction rate will be increase but up to a certain limit.this is substrate concentration

Inhibit the catalytic reaction

What is the Effect of Na2HPo4 as Inhibitor and tris as inhibitor on the Rate of Enzyme Catalyzed Reaction ?