Penicilopepsin

Penicilopepsin
Identifikatori
EC broj 3.4.23.20
CAS broj 2620465
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Penicilopepsin (EC 3.4.23.20, peptidaza A, Penicillium janthinellum aspartinska proteinaza, kiselinska proteaza A, Penicillium citrinum kiselinska proteinaza, Penicillium ciklopium kiselinska proteinaza, Penicillium expansum kiselinska proteinaza, Penicillium janthinellum kiselinska proteinaza, Penicillium expansum aspartinska proteinaza, Penicillium aspartinska proteinaza, Penicillium caseicolum aspartinska proteinaza, Penicillium roqueforti kiselinska proteinaza, Penicillium duponti aspartinska proteinaza, Penicillium citrinum aspartinska proteinaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Hidroliza proteina sa širokom specifičnošću, sličnom pepsinu A. Postoji preferencija za hidrofobne ostatke u P1 i P1', ali takođe dolazi do razlaganja Gly20-Glu u B lancu insulina.

Ovaj enzim je prisutan u gljivi Penicillium janthinellum.

Reference

  1. ↑ Mains, G., Takahashi, M., Sodek, J. and Hofmann, T. (1971). „The specificity of penicillopepsin”. Can. J. Biochem. 49: 1134-1149. PMID 4946839. 
  2. ↑ Zevaco, C., Hermier, J. and Gripon, J.-C. (1973). „Le système protéolytique de Penicillium roqueforti. II - Purification et propriétés de la protéase acide”. Biochimie 55: 1353-1360. PMID 4790849. 
  3. ↑ Emi, S., Myers, D.V. and Iacobucci, G.A. (1976). „Purification and properties of the thermostable acid protease of Penicillium duponti”. Biochemistry 15: 842-848. PMID 2287. 
  4. ↑ Hofmann, T. (1976). „Penicillopepsin”. Methods Enzymol. 45: 434-450. PMID 1012008. 
  5. ↑ Hsu, I.-N., Delbaere, L.T.J., James, M.N.G. and Hofmann, T. (1977). „Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin”. Nature 266: 140-144. PMID 323722. 

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