pp1a cleaves itself

Stable Identifier
Reaction [transition]
Homo sapiens
Related Species
Human SARS coronavirus
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
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The crucial step of autocleavage of pp1a involves the formation of an "intermediate" pp1a dimer which has weak protease activity. This "embedded" 3CLp liberates itself by cleaving the ends off its monomer in trans. Only after that the cleaved 3CLp forms a dimer, the most efficient form of the enzyme (Hsu et al, 2005; Chen et al, 2010; Muramatsu et al, 2016).

Literature References
PubMed ID Title Journal Year
27799534 SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity

Muramatsu, T, Takemoto, C, Kim, YT, Wang, H, Nishii, W, Terada, T, Shirouzu, M, Yokoyama, S

Proc. Natl. Acad. Sci. U.S.A. 2016
15788388 Mechanism of the maturation process of SARS-CoV 3CL protease

Hsu, MF, Kuo, CJ, Chang, KT, Chang, HC, Chou, CC, Ko, TP, Shr, HL, Chang, GG, Wang, AH, Liang, PH

J. Biol. Chem. 2005
21203998 Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode

Chen, S, Jonas, F, Shen, C, Hilgenfeld, R, Higenfeld, R

Protein Cell 2010
Catalyst Activity

cysteine-type endopeptidase activity of pp1a dimer [cytosol]

Orthologous Events
Name Identifier Synonyms
severe acute respiratory syndrome DOID:2945 SARS-CoV infection, SARS
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