Penicillopepsin
| Penicillopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.20 | ||||||||
| CAS number | 2620465 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Penicillopepsin (EC 3.4.23.20, peptidase A, Penicillium janthinellum aspartic proteinase, acid protease A, Penicillium citrinum acid proteinase, Penicillium cyclopium acid proteinase, Penicillium expansum acid proteinase, Penicillium janthinellum acid proteinase, Penicillium expansum aspartic proteinase, Penicillium aspartic proteinase, Penicillium caseicolum aspartic proteinase, Penicillium roqueforti acid proteinase, Penicillium duponti aspartic proteinase, Penicillium citrinum aspartic proteinase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-Glu in the B chain of insulin. Clots milk, and activates trypsinogen
This enzyme is present in fungus Penicillium janthinellum.
References
- ↑ Mains, G.; Takahashi, M.; Sodek, J.; Hofmann, T. (1971). "The specificity of penicillopepsin". Can. J. Biochem. 49: 1134–1149. PMID 4946839. doi:10.1139/o71-164.
- ↑ Zevaco, C.; Hermier, J.; Gripon, J.-C. (1973). "Le système protéolytique de Penicillium roqueforti. II - Purification et propriétés de la protéase acide". Biochimie. 55: 1353–1360. PMID 4790849. doi:10.1016/s0300-9084(74)80543-2.
- ↑ Emi, S.; Myers, D.V.; Iacobucci, G.A. (1976). "Purification and properties of the thermostable acid protease of Penicillium duponti". Biochemistry. 15: 842–848. PMID 2287. doi:10.1021/bi00649a018.
- ↑ Hofmann, T. (1976). "Penicillopepsin". Methods Enzymol. 45: 434–450. PMID 1012008. doi:10.1016/s0076-6879(76)45038-3.
- ↑ Hsu, I.-N.; Delbaere, L.T.J.; James, M.N.G.; Hofmann, T. (1977). "Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin". Nature. 266: 140–144. PMID 323722. doi:10.1038/266140a0.
External links
- Penicillopepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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