EC |
3.4.23.20 |
Accepted name: |
penicillopepsin |
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 |
Other name(s): |
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 |
Comments: |
From the imperfect fungus Penicillium janthinellum. In peptidase family A1 (pepsin A family). Closely related enzymes have been isolated from P. roqueforti [2] and P. duponti [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-08-2 |
References: |
1. |
Mains, G., Takahashi, M., Sodek, J. and Hofmann, T. The specificity of penicillopepsin. Can. J. Biochem. 49 (1971) 1134–1149. [PMID: 4946839] |
2. |
Zevaco, C., Hermier, J. and Gripon, J.-C. Le système protéolytique de Penicillium roqueforti. II - Purification et propriétés de la protéase acide. Biochimie 55 (1973) 1353–1360. [PMID: 4790849] |
3. |
Emi, S., Myers, D.V. and Iacobucci, G.A. Purification and properties of the thermostable acid protease of Penicillium duponti. Biochemistry 15 (1976) 842–848. [PMID: 2287] |
4. |
Hofmann, T. Penicillopepsin. Methods Enzymol. 45 (1976) 434–450. [DOI] [PMID: 1012008] |
5. |
Hsu, I.-N., Delbaere, L.T.J., James, M.N.G. and Hofmann, T. Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin. Nature 266 (1977) 140–144. [PMID: 323722] |
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[EC 3.4.23.20 created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992)] |
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