Kaspaza-2
| Kaspaza-2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.22.55 | ||||||||
| CAS broj | 182372-14-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Kaspaza-2 (EC 3.4.22.55, ICH-1, NEDD-2, kaspaza-2L, kaspaza-2S, CASP-2, NEDD2 protein) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Neophodno je prisustvo Asp ostatka u P1 poziciji, pri čemu je Asp316 esencijalan za proteolitičku aktivnost. Preferentno dolazi do razlaganja sekvence Val-Asp-Val-Ala-Asp-
Kaspaze-2 je inicijator kaspaze, kao i kaspaza-8 (EC 3.4.22.61), kaspaza-9 (EC 3.4.22.62) i kaspaza-10 (EC 3.4.22.63).
Reference
- ↑ Kumar, S., Kinoshita, M., Noda, M., Copeland, N.G. and Jenkins, N.A. (1994). „Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme”. Genes Dev. 8: 1613-1626. PMID 7958843.
- ↑ Wang, L., Miura, M., Bergeron, L., Zhu, H. and Yuan, J. (1994). „Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death”. Cell 78: 739-750. PMID 8087842.
- ↑ 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.
- ↑ Mancini, M., Machamer, C.E., Roy, S., Nicholson, D.W., Thornberry, N.A., Casciola-Rosen, L.A. and Rosen, A. (2000). „Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis”. J. Cell Biol. 149: 603-612. PMID 10791974.
- ↑ Zhivotovsky, B. and Orrenius, S. (2005). „Caspase-2 function in response to DNA damage”. Biochem. Biophys. Res. Commun. 331: 859-867. PMID 15865942.
- ↑ 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.
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 Caspase-2
- 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
