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Literature summary for 3.4.22.69 extracted from

  • Muramatsu, T.; Kim, Y.T.; Nishii, W.; Terada, T.; Shirouzu, M.; Yokoyama, S.
    Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins (2013), FEBS J., 280, 2002-2013.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme stimulation occurs in two steps, with approximately 8fold stimulation by N-terminal cleavage, approximately 4fold stimulation by C-terminal cleavage, and 23fold stimulation by the cleavage of both termini, compared to the pro-form with both the N- and C-terminal pro-sequences Severe acute respiratory syndrome-related coronavirus

Protein Variants

Protein Variants Comment Organism
additional information development of a SARS 3CL protease autoprocessing system by use of the Escherichia coli cell-free protein synthesis system, with the N- and C-terminal 10 amino acid pro-sequences accompanied by an S-tag and a His-tag, respectively Severe acute respiratory syndrome-related coronavirus
Q1N site-directed mutagenesis, the mutation results in loss of cleavage at this site Severe acute respiratory syndrome-related coronavirus
Q306N site-directed mutagenesis, the mutation results in loss of cleavage at this site Severe acute respiratory syndrome-related coronavirus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
2 * 34000, mature, catalytically active enzyme, SDS-PAGE, SARS-CoV 3CLpro exists as a homodimer, in which each protomer has an active site Severe acute respiratory syndrome-related coronavirus

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the enzyme self-activates via autoprocessing, analysis using enzyme pro-forms with the N-terminal pro-sequence, the C-terminal pro-sequence or both pro-sequences as catalyst toward the pro-form with both N- and C-terminal pro-sequences, mechanism, overview. The stimulation occurs in two steps, with approximately 8fold stimulation by N-terminal cleavage, approximately 4fold stimulation by C-terminal cleavage, and 23fold stimulation by the cleavage of both termini, compared to the pro-form with both the N- and C-terminal pro-sequences. Such cleavage mainly occurs in a trans manner, i.e. the pro-form dimer cleaves the monomeric form. C-terminal cleavage is due to removal of its trans (inter-dimer) inhibitory effect Severe acute respiratory syndrome-related coronavirus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs autoprocessing, overview. As 3CLpro requires a glutamine residue at the P1 position of the substrate Severe acute respiratory syndrome-related coronavirus ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 34000, mature, catalytically active enzyme, SDS-PAGE, SARS-CoV 3CLpro exists as a homodimer, in which each protomer has an active site Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms Comment Organism
3C-like protease
-
Severe acute respiratory syndrome-related coronavirus
3cLpro
-
Severe acute respiratory syndrome-related coronavirus
main protease
-
Severe acute respiratory syndrome-related coronavirus
Mpro
-
Severe acute respiratory syndrome-related coronavirus
SARS 3CL protease
-
Severe acute respiratory syndrome-related coronavirus
SARS-CoV 3CLpro
-
Severe acute respiratory syndrome-related coronavirus
severe acute respiratory syndrome coronavirus 3C-like protease
-
Severe acute respiratory syndrome-related coronavirus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
autocatalytic assay at Severe acute respiratory syndrome-related coronavirus

General Information

General Information Comment Organism
additional information autoprocessing mechanism of the enzyme Severe acute respiratory syndrome-related coronavirus