Rutvi

As seen in the graph above, as substance concentration increases, the amount of product
produced in mgdm-3 increases as well. The results of enzyme activity in the solution without
inhibitors shows the maximum amount of products that can be produced up until a
substrate concentration of 250 mgdm-3, which we can call Pmax. As seen on the graph, both
trendlines of inhibitor A, that of 2% and of 5%, do not seem to be reaching Pmax, or the
maximum amount of product produced. This indicates that inhibitor A is a non-competitive
inhibitor: a non-competitive inhibitor binds to an allosteric site on the enzyme, thus
changing the conformation of the active site, which means that the substrate cannot bind to
the active site and therefore cannot be broken down to form the products. The higher the
concentration of the inhibitor (inhibitor A), the more likely it is for the inhibitor to bind to an
allopathic site, so less products are formed. This is shown on the graph by the difference in
the amount of product produced by inhibitor A in a concentration of 2% and of 5%: as
displayed, the higher the concentration of inhibitors, the lower the amount of products
produced. On the other hand, both trendlines of inhibitor B, that of 2% and of 5%, are rising
closer to Pmax with increasing substrate concentration. This indicates that inhibitor B is a
competitive inhibitor: a competitive inhibitor competes with the substrate to bind to the
active site, which does not allow the substrate to be broken down into the products and as
substrate concentration increases, the effect of the inhibitor is reduced as there are more
chances of the enzyme successfully colliding with a substrate molecule, therefore more of
the products are formed. As the graph shows, inhibitor B of both concentrations are close to
Pmax at 250 mgdm-3, and we can predict that at higher substrate concentrations, it will
eventually reach the same number of products formed as the solution without an inhibitor,
just at a flatter slope.