In Experiment 1, the enzyme was mixed with three different compounds, A, B, and C. These mixtures were set at varying temperatures and the concentrations of product recorded. The optimal temperature for this enzyme is between 37˚C and 39˚C. The amount of product at this temperature range exceeds the amount of product at all other temperatures indicating that the enzyme retains an optimal shape and is most efficient at this temperature range. At other temperatures, the H-bonds holding the enzyme together come apart which changes the shape of the molecule.
The optimal pH (see data from experiment 2) is 7 for this enzyme. The amount of product found at this pH far exceeded all other levels of pH. At other pH levels, it is possible that high H+ or OH- concentrations affect the side chains of the enzyme which puts it at risk for acidosis and changes its shape and makes it less effective at binding to the substrate.
From experiments 3 and 4 it is concluded that compound A is the substrate, compound C is neither substrate, inhibitor, nor co-enzyme and compound B is a necessary co-enzyme. In experiment 3 there was no reaction, primarily because this enzyme requires the presence of compound B (the co-enzyme) to overcome the activation energy. That is why there was no reaction even though both enzyme and substrate (compound A) were present. It is important to note that compound B stays relatively constant throughout the reaction; This is because enzymes are not consumed in chemical reactions. Experiment 4 represents the successful completion of the reaction. Both enzymes were present, thus as substrate decreased (due to conversion) product increased.
From experiment 5, it is concluded that substance D is an inhibitor. Substance D decreases at the same rate that substance A is decreasing. Substance D is binding to substance A. This reaction between substances A and D prevents the interaction between the unknown enzyme, substance A and the co-enzyme (substance B). Thus there is no change in the concentrations of B and C. The amount of product follows an inverse curve to the substrate and the inhibitor. This is the result of the reaction of the inhibitor and the substrate; as more of the substrate is consumed in this reaction, less of it is available for conversion into product. In the end, nearly all substrate is consumed by the inhibitor and cannot be converted to product.