| Official Name |
| Deuterolysin.
|
| Alternative Name(s) |
| Acid metalloproteinase. |
| Microbial neutral proteinase II. |
| Penicillium roqueforti protease II. |
| Reaction catalysed |
| Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain |
| Cofactor(s) |
| Zinc.
|
| Comment(s) |
- Proteolytic activity found in Penicillium roqueforti, P.caseicolum,
Aspergillus sojae and A.oryzae.
- Optimum pH of 5 for digesting various proteins.
- Strong action on protamine and histones.
- Insensitive to phosphoramidon.
- A distinct A.sojae endopeptidase is larger and has neutral pH
optimum.
- Belongs to peptidase family M35.
- Formerly EC 3.4.24.4.
|
| Cross-references |
| PROSITE | PDOC00129 |
| BRENDA | 3.4.24.39 |
| PUMA2 | 3.4.24.39 |
| PRIAM enzyme-specific profiles | 3.4.24.39 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.24.39 |
| IUBMB Enzyme Nomenclature | 3.4.24.39 |
| IntEnz | 3.4.24.39 |
| MEDLINE | Find literature relating to 3.4.24.39 |
| MetaCyc | 3.4.24.39 |
| UniProtKB/Swiss-Prot |
|