Abstract:
:Sequence comparisons have recently shown that the Schistosoma mansoni protein Sm32 is similar to asparaginyl endoproteinases, a novel family of cysteine proteinases, of which the legumains from 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 adult S. mansoni. The S. mansoni activity 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.
journal_name
Parasitologyjournal_title
Parasitologyauthors
Dalton JP,Hola-Jamriska L,Brindley PJdoi
10.1017/s0031182000077052subject
Has Abstractpub_date
1995-12-01 00:00:00pages
575-80eissn
0031-1820issn
1469-8161journal_volume
111 ( Pt 5)pub_type
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