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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. 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 Gly-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). "". 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". Part B: Proteolytic Enzymes. Methods in Enzymology. Vol. 45. pp. 434–52. doi:10.1016/s0076-6879(76)45038-3. ISBN 978-0-12-181945-3. 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. Bibcode:1977Natur.266..140H. doi:10.1038/266140a0. PMID 323722.

External links

• Penicillopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.23