A number of potential targets for the development of new therapeutics to treat human disease are now readily provided by genomics and proteomics. Proteins are the main targets for drug or vaccine discovery and amongst them proteases constitute one of the main classes. Proteases became economically important drug targets upon the realization that, besides their primary function in the hydrolysis of peptide bonds, they were extremely important signalling molecules involved in numerous vital processes. According to bioinformatics analysis of the human genome, 566 proteases had been identified so far. Of these, 273 have been found in extracellular compartments or in the lumen of secretory compartments, 277 in intracellular compartments, and 16 in the cell membrane at the surface. The focus of this review will be on extracellular proteases (ECP), a complex and heterogenous family of enzymes. Compared to lipase and amylase, which break down fats and carbohydrates, respectively, the protease family has more extensive roles.  Yes, protease helps break down protein in food into amino acids, which the body can then use for energy, but where proteases stand apart is the fact that they also play a number of other roles in essential processes, such as: Blood clotting, Cell division, Recycling of proteins, Immune support. In some cases, enzymes are directly responsible for activating these processes, and in other cases, they speed them up to the point where they have a notable effect.  Studies are also showing that getting added protease may have some potential health benefits. Both plants and animals have proteases, and in some cases, incorporating plant enzymes is a great option.