Kokolizin
| Kokolizin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.24.30 | ||||||||
| CAS broj | 156859-08-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Kokolizin (EC 3.4.24.30, Streptococcus thermophilus intracelularna proteinaza, EM 19000) je enzim.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Preferentno razlaganje: -Leu, -Phe, -Tyr, -Ala
Ova endopeptidaza je prisutna u bakterijama S. thermophilus i S. Diacetilactis, kao i u medijumu bakterije S. Faecalis.
Reference
- ↑ Desmazeaud, M.J. (1974). „Propriétés générales et spécificité d’action d’une endopeptidase neutre intracellulaire de Streptococcus thermophilus”. Biochimie 56: 1173-1181. PMID 4451671.
- ↑ Desmazeaud, M.J. and Zevaco, C. (1976). „General properties and substrate specificity of an intracellular neutral protease from Streptococcus diacetilactis'”. Ann. Biol. Anim. Biochem. Biophys. 16: 851-868.
- ↑ Smith, R.A.G., Green, J. and Kopper, P.H. (1980). „The purification and properties of a fibrinolytic neutral metalloendopeptidase from Streptococcus faecalis”. Arch. Biochem. Biophys. 202: 629-638. PMID 6779709.
- ↑ Mäkinen, P.-L., Clewell, D.B., An, F., Mäkinen, K.K. (1989). „P'urification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10)”. J. Biol. Chem. 264: 3325-3334. PMID 2536744.
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 Coccolysin
- 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
