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Proteases serve diverse biological functions using a few basic mechanisms, having evolved from a common ancestral gene through gene duplication and divergent evolution.
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Evolutionary conservation of protease mechanisms may aid cardiovascular drug design; leaves open clinical translation pending targeted studies.
One of the striking features of the proteolytic enzymes as a group is the immense variety of biological functions served by enzymes employing one of a few basic mechanisms. For example, in the higher animals, enzymes for activation of zymogens (trypsin), for digestion of dietary proteins (trypsin, chymotrypsin, elastase), for blood clotting (thrombin), for clot lysis (plasmin), and for sensing pain (kallikrein) all appear to use the same mechanism and to have evolved from the same ancestral gene by the process of gene duplication and subsequent divergent evolution. Equally striking is the variety of chemical solutions of the same functional problem, such as the peptide-bond cleavage by sulfhydryl proteases on the one hand and serine proteases on the other.
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Neurath et al. (1967) studied this question. Proteases serve diverse biological functions using a few basic mechanisms, having evolved from a common ancestral gene through gene duplication and divergent evolution.
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