Penicillopepsin Explained
Penicillopepsin |
Ec Number: | 3.4.23.20 |
Cas Number: | 2620465 |
Penicillopepsin (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.
Notes and References
- Mains G, Takahashi M, Sodek J, Hofmann T . The specificity of penicillopepsin . Canadian Journal of Biochemistry . 49 . 10 . 1134–49 . October 1971 . 4946839 . 10.1139/o71-164 .
- Zevaco C, Hermier J, Gripon JC . [Proteolytic system in ''Penicillium roqueforti''. 2. Purification and properties of acid protease] . Biochimie . 55 . 11 . 1353–60 . 1973 . 4790849 . 10.1016/s0300-9084(74)80543-2 .
- Emi S, Myers DV, Iacobucci GA . Purification and properties of the thermostable acid protease of Penicillium duponti . Biochemistry . 15 . 4 . 842–8 . February 1976 . 2287 . 10.1021/bi00649a018 .
- Book: Hofmann T . Penicillopepsin . Part B: Proteolytic Enzymes . Methods in Enzymology . 45 . 434–52 . 1976 . 1012008 . 10.1016/s0076-6879(76)45038-3 . 978-0-12-181945-3 .
- Hsu IN, Delbaere LT, James MN, Hofmann T . Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin . Nature . 266 . 5598 . 140–5 . March 1977 . 323722 . 10.1038/266140a0 . 1977Natur.266..140H .