Kaspaza-8
(Preusmjereno sa stranice ICE-slična apoptotička proteaza 5)
Kaspaza-8 (EC 3.4.22.61, FLICE, FADD-sličan ICE, MACH, MORT1-asocirani CED-3 homolog, Mch5, sisarski Ced-3 homolog 5, CASP-8, ICE-slična apoptotička proteaza 5, FADD-homologna ICE/CED-3-slična proteaza, apoptotička cisteinska proteaza, apoptotička proteaza Mch-5, CAP4) je enzim.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Kaspaza-8 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.22.61 | ||||||||
| CAS broj | 179241-78-2 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- Neophodno je prisustvo Asp ostatka u P1 poziciji. Preferentno dolazi do razlaganja sekvence (Leu/Asp/Val)-Glu-Thr-Asp-(Gly/Ser/Ala)
Kaspaza-8 je efektor/izvršilac kaspaze, kao što su i kaspaza-2 (EC 3.4.22.55), kaspaza-9 (EC 3.4.22.62) i kaspaza-10 (EC 3.4.22.63).
Reference
uredi- ↑ Chang, H.Y. and Yang, X. (2000). „Proteases for cell suicide: functions and regulation of caspases”. Microbiol. Mol. Biol. Rev. 64: 821-846. PMID 11104820.
- ↑ Boldin, M.P., Goncharov, T.M., Goltsev, Y.V. and Wallach, D. (1996). „Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death”. Cell 85: 803-815. PMID 8681376.
- ↑ Muzio, M., Chinnaiyan, A.M., Kischkel, F.C., O'Rourke, K., Shevchenko, A., Ni, J., Scaffidi, C., Bretz, J.D., Zhang, M., Gentz, R., Mann, M., Krammer, P.H., Peter, M.E. and Dixit, V.M. (1996). „FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex”. Cell 85: 817-827. PMID 8681377.
- ↑ Salvesen, G.S. and Boatright, K.M. (2004). „Caspase-8”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes (2nd izd.). London: Elsevier. str. 1293-1296.
- ↑ Fischer, U., Stroh, C. and Schulze-Osthoff, K. (2006). „Unique and overlapping substrate specificities of caspase-8 and caspase-10”. Oncogene 25: 152-159. PMID 16186808.
- ↑ Blanchard, H., Donepudi, M., Tschopp, M., Kodandapani, L., Wu, J.C. and Grütter, M.G. (2000). „Caspase-8 specificity probed at subsite S(4): crystal structure of the caspase-8-Z-DEVD-cho complex”. J. Mol. Biol. 302: 9-16. PMID 10964557.
- ↑ Boatright, K.M., Deis, C., Denault, J.B., Sutherlin, D.P. and Salvesen, G.S. (2004). „Activation of caspases-8 and -10 by FLIPL”. Biochem. J. 382: 651-657. PMID 15209560.
Literatura
uredi- 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.
- Salvesen, G.S. and Boatright, K.M. (2004). „Caspase-8”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes (2nd izd.). London: Elsevier. str. 1293-1296.