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Literature summary for 3.4.22.69 extracted from

  • Zhong, N.; Zhang, S.; Zou, P.; Chen, J.; Kang, X.; Li, Z.; Liang, C.; Jin, C.; Xia, B.
    Without its N-finger, the main protease of severe acute respiratory syndrome coronavirus can form a novel dimer through its C-terminal domain (2008), J. Virol., 82, 4227-4234.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information without the N-finger, SARS-CoV Mpro can no longer retain the active dimer structure. It can form a new type of dimer which is inactive. Therefore, the N-finger of SARS-CoV Mpro is not only critical for its dimerization but also essential for the enzyme to form the enzymatically active dimer Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
MCAAVLQSGFR-Lys(Dnp)-Lys-NH2 + H2O
-
 Severe acute respiratory syndrome-related coronavirus MCAAVLQ + Ser-Gly-Phe-Arg-Lys(Dnp)-Lys-NH2
-
 ?

Subunits

Subunits Comment Organism
dimer SARS-CoV Mpro exists in solution as an equilibrium of both monomeric and dimeric forms, and the dimeric form is the enzymatically active form Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms Comment Organism
SARS-CoV Mpro
-
 Severe acute respiratory syndrome-related coronavirus