CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.60 | Sandwich |
|
2.60.120 | Jelly Rolls |
|
2.60.120.700 | Peptidase G1 |
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 | 1S2B |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
Proc.Natl.Acad.Sci.USA
|
