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

  1. ↑ Mains G, Takahashi M, Sodek J, Hofmann T (October 1971). "The specificity of penicillopepsin". Canadian Journal of Biochemistry. 49 (10): 1134–49. doi:10.1139/o71-164. PMID 4946839.
  2. ↑ Zevaco C, Hermier J, Gripon JC (1973). "[Proteolytic system in Penicillium roqueforti. 2. Purification and properties of acid protease]". Biochimie. 55 (11): 1353–60. doi:10.1016/s0300-9084(74)80543-2. PMID 4790849.
  3. ↑ Emi S, Myers DV, Iacobucci GA (February 1976). "Purification and properties of the thermostable acid protease of Penicillium duponti". Biochemistry. 15 (4): 842–8. doi:10.1021/bi00649a018. PMID 2287.
  4. ↑ Hofmann T (1976). "Penicillopepsin". Methods in Enzymology. 45: 434–52. doi:10.1016/s0076-6879(76)45038-3. PMID 1012008.
  5. ↑ Hsu IN, Delbaere LT, James MN, Hofmann T (March 1977). "Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin". Nature. 266 (5598): 140–5. doi:10.1038/266140a0. PMID 323722.
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