The Enzyme Database

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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. [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]
[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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