Z-KAGG-AMC
Coronaviruses (CoVs) can infect humans and multiple species of animals, causing a wide spectrum of diseases. In late 2019, a novel coronavirus, termed severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was determined as a cause for several cases of respiratory disease (Covid-19). Even though most infected patients only suffer from mild symptoms such as fever and cough associated with a good prognosis, the disease can progress into fatal cases of pneumonia and acute respiratory failure, especially in older males with comorbidities. Covid-19 rapidly spread worldwide. As of May 31st, 2022, more than 6.2 million people have died from coronavirus worldwide, and ~530 million cases have been reported. Coronavirus is a single-stranded RNA positive-strand envelope type B coronavirus. Like the other two coronaviruses that cause SARS (Severe Acute Respiratory Syndrome) and MERS (Middle East Respiratory Syndrome), SARS-CoV-2 encodes non-structural, structural, and accessory proteins. Non-structural proteins include 3-chymotrypsin-like protease (3CLpro), papain-like protease, helicase, and RNA-dependent RNA polymerase (RNA -dependent RNA polymerase (RdRp). Structural proteins include spike glycoproteins. Papain in coronavirus operates on more than 11 cleavage sites on the large polyprotein 1ab. Processing of polyproteins translated from viral RNA is essential, therefore, the main proteases are identified as an attractive drug targets for preventing virus imitation. Papain-like protease (PLpro) of coronaviruses carries out proteolytic maturation of non-structural proteins that play a role in replication of the virus and performs deubiquitination of host cell factors to scuttle antiviral responses. Z-KAGG-AMC is cleaved by papain-like proteases to give the highly fluorescent AMC product. The fluorescence intensity of released AMC is proportional to the protease activity. Z-KAGG-AMC might be used for screening and studying kinetics of PLpro inhibitors.
Spectrum
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Product family
Name | Excitation (nm) | Emission (nm) |
Z-DEVD-AMC | 341 | 441 |
Z-LRGG-AMC | 341 | 441 |
Z-KKAG-AMC | 341 | 441 |
References
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Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease.
Authors: Ratia, Kiira and Kilianski, Andrew and Baez-Santos, Yahira M and Baker, Susan C and Mesecar, Andrew
Journal: PLoS pathogens (2014): e1004113
Authors: Ratia, Kiira and Kilianski, Andrew and Baez-Santos, Yahira M and Baker, Susan C and Mesecar, Andrew
Journal: PLoS pathogens (2014): e1004113
Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease.
Authors: Lindner, Holger A and Lytvyn, Viktoria and Qi, Hongtao and Lachance, Paule and Ziomek, Edmund and Ménard, Robert
Journal: Archives of biochemistry and biophysics (2007): 8-14
Authors: Lindner, Holger A and Lytvyn, Viktoria and Qi, Hongtao and Lachance, Paule and Ziomek, Edmund and Ménard, Robert
Journal: Archives of biochemistry and biophysics (2007): 8-14
The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity.
Authors: Barretto, Naina and Jukneliene, Dalia and Ratia, Kiira and Chen, Zhongbin and Mesecar, Andrew D and Baker, Susan C
Journal: Journal of virology (2005): 15189-98
Authors: Barretto, Naina and Jukneliene, Dalia and Ratia, Kiira and Chen, Zhongbin and Mesecar, Andrew D and Baker, Susan C
Journal: Journal of virology (2005): 15189-98
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