levels to allow cells to survive. When G6PD's substrate concentration is high, uncompetitive inhibition of the enzyme becomes far more effective. As substrate concentration increases, the amount of ES complex increases as well, and with more ES complex to bind, uncompetitive inhibitors become far more active. This inhibition works such that the higher the concentration of substrate is in the system initially, the harder it is to reach the maximum velocity of the reaction. At low initial substrate concentrations, increasing the concentration of substrate is sometimes enough to entirely or even fully restore the enzyme's function, but as soon as initial concentration increases past a certain point, reaching the maximal enzyme velocity is all but impossible. This extreme sensitivity to substrate concentration within the cancer mechanism implicates uncompetitive inhibition rather than mixed inhibition, which displays similar traits but is often less sensitive to substrate concentration due to some inhibitor binding to free enzymes regardless of the substrate's presence. As such, the extreme strength of uncompetitive inhibitors at high substrate concentrations and the overall sensitivity to substrate amount indicates that only uncompetitive inhibition can make this type of process possible. Importance in cell and organelle membranes Although this form of inhibition is present in various diseases within biological systems, it does not necessarily only relate to pathologies. It can be involved in typical bodily functions. For example, active sites capable of uncompetitive inhibition appear to be present in membranes, as removing lipids from cell membranes and making active sites more accessible through conformational changes has been shown to invoke elements resembling the effects of uncompetitive inhibition (i.e. both KM and VMax decrease). In mitochondrial membrane lipids specifically, removing lipids decreases the alpha-helix content in mitochondria and leads to changes in ATPase resembling uncompetitive inhibition. This presence of uncompetitive enzymes in membranes has also been supported in a number of other studies. A type of protein called an Arf protein involved in regulating membrane activity was being studied, and it was found that an inhibitor called BFA trapped one of Arf's intermediates via uncompetitive inhibition. This made it clear that this type of inhibition exists within various types of cells and organelles as opposed to just in pathological cells. In fact, BFA was found to relate to the activity of the Golgi apparatus and its role in regulating movement across the cell membrane. Presence in the cerebellar granule layer Uncompetitive inhibition can