Kaspaza-3

Kaspaza-3
Kaspaza-3 heterotetramer, Human
Identifikatori
EC broj 3.4.22.56
CAS broj 169592-56-7
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Pretraga
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PubMed articles
NCBI Protein search

Kaspaza-3 (EC 3.4.22.56, CPP32, apopain, jama protein) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

Neophodno je prisustvo Asp ostatka u pozicijama P1 i P4. Preferentno dolazi do razlaganja sekvence Asp-Xaa-Xaa-Asp- sa hidrofobnim aminokiselinskim ostatkom u P2 poziciji i hidrofilnim aminokiselinskim ostatkom u P3, mada Val ili Ala takođe mogu da budu u toj poziciji

Kaspaza-3 je efektor/izvršilac kaspaze, kao što su i kaspaza-6 (EC 3.4.22.59) i kaspaza-7 (EC 3.4.22.60).

Reference

  1. ↑ Krebs, J.F., Srinivasan, A., Wong, A.M., Tomaselli, K.J., Fritz, L.C. and Wu, J.C. (2000). „Heavy membrane-associated caspase 3: identification, isolation, and characterization”. Biochemistry 39: 16056-16063. PMID 11123933. 
  2. ↑ Li, H., Bergeron, L., Cryns, V., Pasternack, M.S., Zhu, H., Shi, L., Greenberg, A. and Yuan, J. (1997). „Activation of caspase-2 in apoptosis”. J. Biol. Chem. 272: 21010-21017. PMID 9261102. 
  3. ↑ Nicholson, D. and Thornberry, N.A. (2004). „Caspase-3 and caspase-7”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes (2nd izd.). London: Elsevier. str. 1298-1302. 
  4. ↑ Fang, B., Boross, P.I., Tozser, J. and Weber, I.T. (2006). „Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition”. J. Mol. Biol. 360: 654-666. PMID 16781734. 
  5. ↑ 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. 
  6. ↑ Martin, S.J., Amarante-Mendes, G.P., Shi, L., Chuang, T.H., Casiano, C.A., O'Brien, G.A., Fitzgerald, P., Tan, E.M., Bokoch, G.M., Greenberg, A.H. and Green, D.R. (1996). „The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism”. EMBO J. 15: 2407-2416. PMID 8665848. 

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. 
  • Nicholson, D. and Thornberry, N.A. (2004). „Caspase-3 and caspase-7”. u: Barrett, A.J., Rawlings, N.D. and Woessner, J.F.. Handbook of Proteolytic Enzymes (2nd izd.). London: Elsevier. str. 1298-1302. 

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