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A classification of proteolytic enzymes


, : A classification of proteolytic enzymes. Advances En Zymol 2: 49-68

Recent exptl. data showed that the older classification of proteolytic enzymes based on the chain-length and ionization of the substrate required revision. Data were obtained using low molecular wt. substrates. Proteolytic enzymes were classified as exopeptidases (pepti-dases) and as endopeptidases (proteinases). The specificity of each enzyme depended on specific amino acid groupings within the substrate molecules, e.g., pepsin and chymo-trypsin required the presence of a tyrosine or phenylalanine residue. Various tissues produced enzymes which exhibited an identical specificity type. Papain, trypsin and various cathepsins all hydrolyzed benzoyl-1-arginineamide and benzoyl-1-lysineamide. These two substrates were hydrolyzed at the same relative rates by these very different enzymes. Such a group of enzymes was called homospecific. Other examples of homospecific enzymes were given. The activation of intracellular enzymes was described.

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