| Polyporopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.29 | ||||||||
| CAS no. | 61573-73-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Polyporopepsin (EC 3.4.23.29, Polyporus aspartic proteinase, Irpex lacteus aspartic proteinase, Irpex lacteus carboxyl proteinase B) is an enzyme. This enzyme catalyses the following chemical reaction
- Milk clotting activity, broad specificity, but fails to cleave Leu-Tyr or Tyr-Leu of insulin B chain
This enzyme is isolated from the basidiomycete Polyporus tulipiferae.
References
- Kobayashi H, Kusakabe I, Murakami K (1983). "Substrate specificity of a carboxyl proteinase from Irpex lacteus". Agric. Biol. Chem. 47 (8): 1921–1923. doi:10.1271/bbb1961.47.1921.
- Kobayashi H, Sekibata S, Shibuya H, Yoshida S, Kusakabe I, Murakami K (1989). "Cloning and sequence analysis of cDNA for Irpex lacteus aspartic proteinase". Agric. Biol. Chem. 53 (7): 1927–1933. doi:10.1271/bbb1961.53.1927.
External links
- Polyporopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Proteases: aspartate proteases (EC 3.4.23) | |
|---|---|
| Vertebrate | |
| Pathogenic | |
| Plant | |
| Cathepsin | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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