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
- ↑ Mains, G., Takahashi, M., Sodek, J. and Hofmann, T. (1971). „The specificity of penicillopepsin”. Can. J. Biochem. 49: 1134-1149. PMID 4946839.
- ↑ 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.
- ↑ 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.
- ↑ Hofmann, T. (1976). „Penicillopepsin”. Methods Enzymol. 45: 434-450. PMID 1012008.
- ↑ 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.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Penicillopepsin
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
