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ENZYME

ENZYME entry: EC 3.4.23.32

PURL: https://purl.expasy.org/enzyme/EC/3.4.23.32
Accepted Name
scytalidopepsin B
Alternative Name(s)
Scytalidium aspartic proteinase B
Reaction catalysed
Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin
Comment(s)
  • Isolated from the imperfect fungus Scytalidium lignicolum.
  • A second endopeptidase from S.lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate.
  • 1,2-epoxy-3-(p-nitrophenoxy)propane reacts with Glu-53, which replaces one of the aspartic residues at the active center.
  • One of the smallest aspartic endopeptidases active as the monomer, with molecular weight 22 kDa.
  • Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes and Ganoderma lucidum, and in Polyporus tulipiferae (a second endopeptidase distinct from polyporopepsin), but these are of typical aspartic endopeptidase size.
  • Belongs to peptidase family G1.
Cross-references
BRENDA3.4.23.32
EC2PDB3.4.23.32
ExplorEnz3.4.23.32
KEGG Ligand Database for Enzyme Nomenclature3.4.23.32
IUBMB Enzyme Nomenclature3.4.23.32
MEDLINEFind literature relating to 3.4.23.32
MetaCyc3.4.23.32
Rhea expert-curated reactions3.4.23.32
UniProtKB/Swiss-Prot
P15369, PRTB_SCYLI

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