If an enzyme with no inhibitor has a Vmax of .091 abs/min and a Km of .31 mM. An inhibitor is added (1 uM) which changes the Vmax to .036 abs/min and a Km of .13 mM, so it has a Ki of -1.72 and a Ki’ of .65 uM. A substrate is added, which will react with the enzyme to form a toxic product, if it reacts with the enzyme. If they do not react the substrate concentration will slowly reduce via other (safe) pathways. By comparing Km Vmax Ki and Ki’ this inhibitor adaquetly prevent the production of product if the substrate is added below its saturation level?