CATH Classification

Domain Context

CATH Clusters

Superfamily Peptidase G1
Functional Family

Enzyme Information

3.4.23.32
Scytalidopepsin B.
based on mapping to UniProt P15369
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.
-!- 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.

UniProtKB Entries (1)

P15369
PRTB_SCYLI
Scytalidium lignicola
Scytalidopepsin B

PDB Structure

PDB 1S2K
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
Fujinaga, M., Cherney, M.M., Oyama, H., Oda, K., James, M.N.
Proc.Natl.Acad.Sci.USA