EC Number   |
General Information |
Reference  |
|---|
   3.4.22.69 | physiological function |
the enzyme is required for viral polyprotein processing |
693255 |
| 3.4.22.69 | physiological function |
3CLpro is required for viral replication |
707802 |
| 3.4.22.69 | physiological function |
3CLpro is vital for SARS-coronavirus replication |
710675 |
| 3.4.22.69 | more |
the functional unit of Mpro is a homodimer and each subunit contains a His41-Cys145 catalytic dyad. Presence of a complete substrate-binding pocket and oxyanion hole in both protomers. Reversible substrate-induced dimerization is essential for catalysis, molecular mechanism, overview |
731060 |
| 3.4.22.69 | more |
substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the enzyme, overview |
731320 |
| 3.4.22.69 | physiological function |
the activity of the enzyme toward specific viral protein substrates is required for efficient viral replication |
731320 |
| 3.4.22.69 | more |
autoprocessing mechanism of the enzyme |
731790 |
| 3.4.22.69 | physiological function |
during the formation of the coronaviral replication/transcription complex, essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsps |
752729 |
| 3.4.22.69 | drug target |
combination of thioacetal functional group with decahydroisoquinolin or related fused-ring scaffold would be an approach to design inhibitors for SARS 3CL protease |
752974 |
| 3.4.22.69 | physiological function |
the protease 3CLpro processes the polypeptide translation product from the genomic RNA into the structural and nonstructural protein components vital for the replication and packaging of a new generation of viruses |
753268 |
