Asparaginyl endopeptidase activity in adultSchistosoma mansoni

Abstract

SUMMARYSequence comparisons have recently shown that theSchistosoma mansoniprotein Sm32 is similar to asparaginyl endo-proteinases, a novel family of cysteine proteinases, of which the legumains rom legumes are the best characterized. By synthesizing and employing fluorogenic peptide substrates for the specific detection of asparaginyl endopeptidases, we have identified this type of activity in extracts of adultS. mansoni. TheS. mansoniactivity is similar to that of the legumains in its substrate specificity and sensitivity to thiol inhibitors, but differs in its pH and temperature optima for activity. In contrast, unlike the legumains, the schistosome asparaginyl endopeptidase activity is not activated by the reducing agent dithiothreitol. As suggested for legumains, Sm32 may function in the post-translational modification processes that regulate the activity of other molecules.