SARS koronavirusna glavna proteinaza
| SARS koronavirusna glavna proteinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.4.22.69 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
SARS koronavirusna glavna proteinaza (EC 3.4.22.69, 3cLpro, 3C-slična proteaza, koronavirusna 3C-like proteaza, Mpro, SARS 3C-slična proteaza, SARS koronavirusna 3CL proteaza, SARS koronavirusna glavna peptidaza, SARS-CoV 3CLpro enzim, SARS-CoV glavna proteaza, SARS-CoV Mpro, glavna proteaza koronavirusnog jakog akutnog respiratornog sindroma) je enzim.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Najreaktivniji supstrati su peptidi TSAVLQ-SGFRK-NH2 i SGVTFQ-GKFKK. Oni korespondiju mestima samo presecanja SARS 3C-sličnih proteinaza. Postoji preferencija za supstrate sa Gln u P1 poziciji i Leu u P2 poziciji
Glavna proteaza SARS koronavirusa je ključni enzim u obradi replikaznih poliproteina SARS koronavirusa.
Reference
- ↑ Goetz, D.H., Choe, Y., Hansell, E., Chen, Y.T., McDowell, M., Jonsson, C.B., Roush, W.R., McKerrow, J. and Craik, C.S. (2007). „Substrate specificity profiling and identification of a new class of inhibitor for the major protease of the SARS coronavirus”. Biochemistry 46: 8744-8752. PMID 17605471.
- ↑ Fan, K., Wei, P., Feng, Q., Chen, S., Huang, C., Ma, L., Lai, B., Pei, J., Liu, Y., Chen, J. and Lai, L. (2004). „Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase”. J. Biol. Chem. 279: 1637-1642. PMID 14561748.
- ↑ Akaji, K., Konno, H., Onozuka, M., Makino, A., Saito, H. and Nosaka, K. (2008). „Evaluation of peptide-aldehyde inhibitors using R188I mutant of SARS 3CL protease as a proteolysis-resistant mutant”. Bioorg. Med. Chem. 16: 9400-9408. PMID 18845442.
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 SARS+coronavirus+main+proteinase
- 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
