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Literature summary for 3.4.22.69 extracted from

  • Paasche, A.; Zipper, A.; Schaefer, S.; Ziebuhr, J.; Schirmeister, T.; Engels, B.
    Evidence for substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the SARS-CoV main protease (2014), Biochemistry, 53, 5930-5946.
    View publication on PubMed

Application

Application Comment Organism
drug development coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus infections, including severe acute respiratory syndrome (SARS) Severe acute respiratory syndrome-related coronavirus

Inhibitors

Inhibitors Comment Organism Structure
additional information the low inhibition potencies of known covalently interacting inhibitors may, at least in part, be attributed to insufficient fostering of the proton-transfer reaction Severe acute respiratory syndrome-related coronavirus

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme shows a substrate-induced catalytic mechanism that further enhances its substrate specificity, overview Severe acute respiratory syndrome-related coronavirus ?
-
?

Synonyms

Synonyms Comment Organism
coronavirus M(pro)
-
Severe acute respiratory syndrome-related coronavirus
coronavirus main protease
-
Severe acute respiratory syndrome-related coronavirus
SARS-CoV main protease
-
Severe acute respiratory syndrome-related coronavirus

General Information

General Information Comment Organism
additional information substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the enzyme, overview Severe acute respiratory syndrome-related coronavirus
physiological function the activity of the enzyme toward specific viral protein substrates is required for efficient viral replication Severe acute respiratory syndrome-related coronavirus