Katepsin X
| Katepsin X | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.4.18.1 | ||||||||
| CAS broj | 37217-21-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Katepsin X (EC 3.4.18.1, katepsin B2, karboksipeptidaza cisteinskog tipa, katepsin IV, katepsin Z, kiselina karboksipeptidaza, lizozomalna karboksipeptidaza B) je enzim.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Odvajanje C-terminalnih aminokiselinskih ostataks sa širokom specifičšću, sa odsustvom dejstva na C-terminalnom prolinu. Manifestuje slabu endopeptidaznu aktivnost
Katepsin X je lizozomalna cisteinska peptidaza iz familije C1 (papainske familije).
Reference
- ↑ Nägler, D.K., Zhang, R., Tam, W., Sulea, T., Purisima, E.O. and Ménard, R. (1999). „Human cathepsin X: A cysteine protease with unique carboxypeptidase activity”. Biochemistry 38: 12648-12654. PMID 10504234.
- ↑ Nägler, D.K. and Ménard, R. (1998). „Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions”. FEBS Lett. 434: 135-139. PMID 9738465.
- ↑ Santamaría, I. Velasco, G., Pendás, A.M., Fueyo, A. and López-Otín, C. (1998). „Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location”. J. Biol. Chem. 273: 16816-16823. PMID 9642240.
- ↑ McDonald, J.K. and Ellis, S. (1975). „On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1”. Life Sci. 17: 1269-1276. PMID 577.
- ↑ Otto, K. and Riesenkönig, H. (1975). „Improved purification of cathepsin B1 and cathepsin B2”. Biochim. Biophys. Acta 379: 462-475. PMID 1122298.
- ↑ Ninjoor, V., Taylor, S.L. and Tappel, A.L. (1974). „Purification and characterization of rat liver lysosomal cathepsin B2”. Biochim. Biophys. Acta 370: 308-321. PMID 4429705.
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 Cathepsin+X
- 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
