| Official 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 |
|---|
| PROSITE | PDOC00128 |
| BRENDA | 3.4.23.32 |
| PUMA2 | 3.4.23.32 |
| PRIAM enzyme-specific profiles | 3.4.23.32 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.23.32 |
| IUBMB Enzyme Nomenclature | 3.4.23.32 |
| IntEnz | 3.4.23.32 |
| MEDLINE | Find literature relating to 3.4.23.32 |
| MetaCyc | 3.4.23.32 |
| UniProtKB/Swiss-Prot |
|
ExPASy Home page