Biology:Penicillopepsin

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Penicillopepsin
Identifiers
EC number3.4.23.20
CAS number2620465
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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

  1. "The specificity of penicillopepsin". Canadian Journal of Biochemistry 49 (10): 1134–49. October 1971. doi:10.1139/o71-164. PMID 4946839. 
  2. "[Proteolytic system in Penicillium roqueforti. 2. Purification and properties of acid protease]". Biochimie 55 (11): 1353–60. 1973. doi:10.1016/s0300-9084(74)80543-2. PMID 4790849. 
  3. "Purification and properties of the thermostable acid protease of Penicillium duponti". Biochemistry 15 (4): 842–8. February 1976. doi:10.1021/bi00649a018. PMID 2287. 
  4. Penicillopepsin. Methods in Enzymology. 45. 1976. pp. 434–52. doi:10.1016/s0076-6879(76)45038-3. 
  5. "Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin". Nature 266 (5598): 140–5. March 1977. doi:10.1038/266140a0. PMID 323722. 

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