Kaspaza-3
(Preusmjereno sa stranice 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 | ||||||||
| |||||||||
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).
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- 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.