Kaspaza-8

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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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

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

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ 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. 
  7. ↑ 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

  • 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. 

Spoljašnje veze

  • p
  • r
  • u
TemeTipovi
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