Katepsin K
| Katepsin K | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.22.38 | ||||||||
| CAS broj | 94716-09-3 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Katepsin K (EC 3.4.22.38, katepsin O2) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Široka proteolitička aktivnost na malim molekulima. Glavna odrednica specifičnosti je P2, koji je preferentno Leu, Met > Phe, i odsustvo Arg
Ovaj enzim je prominentno izražen u osteoklastima sisara.
Reference
- ↑ Inaoka, T., Bilbe, G., Ishibashi, O., Tezuka, K., Kumegawa, M. and Kokubo, T. (1995). „Molecular cloning of human cDNA for cathepsin K: Novel cysteine proteinase predominantly expressed in bone”. Biochem. Biophys. Res. Commun. 206: 89-96. PMID 7818555.
- ↑ Bossard, M.J., Tomaszek, T.A., Thompson, S.K., Amegadzie, B.Y., Hanning, C.R., Jones, C., Kurdyla, J.T., McNulty, D.E., Drake, F.H., Gowen, M. and Levy, M.A. (1996). „Proteolytic activity of human osteoclast cathepsin K - Expression, purification, activation, and substrate identification”. J. Biol. Chem. 271: 12517-12524. PMID 8647860.
- ↑ Bromme, D., Klaus, J.L., Okamoto, K., Rasnick, D. and Palmer, J.T. (1996). „Peptidyl vinyl sulphones: A new class of potent and selective cysteine protease inhibitors - S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L”. Biochem. J. 315: 85-89. PMID 8670136.
- ↑ Zhao, B.G., Janson, C.A., Amegadzie, B.Y., D'Alessio, K., Griffin, C., Hanning, C.R., Jones, C., Kurdyla, J., McQueney, M., Qiu, X.Y., Smith, W.W. and Abdel-Meguid, S.S. (1997). „Crystal structure of human osteoclast cathepsin K complex with E-64”. Nature Struct. Biol. 4: 109-111. PMID 9033588.
- ↑ McGrath, M.E., Klaus, J.L., Barnes, M.G. and Brömme, D. (1997). „Crystal structure of human cathepsin K complexed with a potent inhibitor”. Nature Struct. Biol. 4: 105-109. PMID 9033587.
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+K
- 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
