3CLp cleaves pp1a

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Locations in the PathwayBrowser
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Main protease of SARS-CoV-2 (3CLpro, nsp5) cleaves all cleavage sites of pp1a and ppa1b starting with nsp4/5, thus cleaving itself, and all the cytosolic RTC proteins. This is essential for maturation of the viral replicase complex and for making it fully functional (Du et al, 2021).

Literature References
PubMed ID Title Journal Year
34847508 Oxidative stress transforms 3CLpro into an insoluble and more active form to promote SARS-CoV-2 replication

Peng, X, Guo, D, Zheng, K, Xia, W, Wang, N, Cao, L, Yu, T, Xie, Y, Shao, Q, Gao, M, Zou, Y, Du, L, Fang, Q, Pan, JA, Zhao, B

Redox Biol 2021
34437808 Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease

Hinshaw, SM, Windsor, IW, Namchuk, MN, MacDonald, EA, Harrison, SC, Frey, G

ACS Infect Dis 2021
Catalyst Activity

cysteine-type endopeptidase activity of 3CLp dimer [cytosol]

This event is regulated