S'-subsite mapping of endoproteinase Glu/Asp-C from Actinomyces sp.

The S'-subsite specificity of the endoproteinase Glu/Asp-C from Actinomyces sp. was studied by acyl transfer reactions using amino-acid- and peptide-derived nucleophilic amino components. The following results were obtained: 1. The enzyme prefers amino acid amides with hydrophobic side chains in P'i position. In addition, positively charged functions in this position favour S'-P' interactions significantly. 2. Stereospecific binding is a prerequisite for nucleophilic efficiency. 3. Dipeptide amides are more efficient amino components in comparison to free dipeptides whereas oligoglycines show a poor nucleophilic behaviour independent of chain length.