Literature summary for 3.4.22.1 extracted from

Krautz-Peterson, G.; Skelly, P.J.
Schistosome asparaginyl endopeptidase (legumain) is not essential for cathepsin B1 activation in vivo (2008), Mol. Biochem. Parasitol., 159, 54-58.

Search for more literature for 3.4.22.1

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	Schistosome asparaginyl endopeptidase, i.e. legumain, is not essential for cathepsin B1 activation in vivo	Schistosoma mansoni

Cloned(Commentary)

Cloned (Comment)	Organism
SmCB1 expression analysis, expression in Pichia pastoris	Schistosoma mansoni

Protein Variants

Protein Variants	Comment	Organism
additional information	suppression of SmAE expression using RNA interference leads to an accumulation of unprocessed SmCB1 and a corresponding diminution in mature cathepsin B protein and cathepsin B enzyme activity in treated parasites	Schistosoma mansoni

Organism

Organism	UniProt	Comment	Textmining
Schistosoma mansoni	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the protein is synthesized as a large 38 kDa precursor form which is proteolytically cleaved to yield a mature, active 31 kDa enzyme by the asparaginyl endopeptidase SmAE, i.e. schistosome legumain, SmAE is central to SmCB1 processing and activation	Schistosoma mansoni

Synonyms

Synonyms	Comment	Organism
cathepsin B1	-	Schistosoma mansoni
Sm31	-	Schistosoma mansoni
SmCB1	-	Schistosoma mansoni

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Release 2023.1 (January 2023)