ID   3.4.23.32
DE   scytalidopepsin B.
AN   Scytalidium aspartic proteinase B.
CA   Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25,
CA   but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin.
CC   -!- Isolated from the imperfect fungus Scytalidium lignicolum.
CC   -!- A second endopeptidase from S.lignicolum (see scytalidopepsin A) that
CC       is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate.
CC   -!- 1,2-epoxy-3-(p-nitrophenoxy)propane reacts with Glu-53, which
CC       replaces one of the aspartic residues at the active center.
CC   -!- One of the smallest aspartic endopeptidases active as the monomer,
CC       with molecular weight 22 kDa.
CC   -!- Similarly inhibitor-resistant endopeptidases are found in the
CC       basidiomycetes Lentinus edodes and Ganoderma lucidum, and in
CC       Polyporus tulipiferae (a second endopeptidase distinct from
CC       polyporopepsin), but these are of typical aspartic endopeptidase
CC       size.
CC   -!- Belongs to peptidase family G1.
DR   P15369, PRTB_SCYLI ;
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