[Structural characteristics providing for high specificity of enteropeptidase]

The effects of structural modification upon the specificity of enteropeptidase were studied. A variation in the unique specificity of the enzyme was shown to be the result of an autolysis caused by the enzyme's loss of calcium ions. The cleavage sites of the autolysis were determined. A truncated enzyme containing the C-terminal fragment of its heavy chain (466-800 residues) and the intact light chain were shown to be the products of autolysis. The kinetic parameters of the hydrolysis of trypsinogen, a recombinant protein, and a peptide substrate with both forms of enteropeptidase were determined. Conditions were found that can help regulate the transition of the native enzyme into the truncated form. A hypothesis was proposed concerning the autoactivational character of proenteropeptidase processing.