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.
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