EC Number   |
General Information |
Reference |
|---|
   3.4.22.69 | more |
autoprocessing mechanism of the enzyme |
731790 |
| 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 | 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 |
the overall amino-acid sequence identity of SARS-CoV-2 and SARS-CoV is very high (86%). The conservation is noticeable at the polyprotein cleavage sites. All 11 3CLpro sites are highly conserved or identical, inferring that their respective proteases have very similar specificities. The 3CLpro sequence of SARS-CoV-2 has only 12 out of 306 residues different from that of SARS-CoV (identity = 96%). Conserved sequence identity is detected among all 11 SARS-CoV-2 genomes SARS-CoV-2 |
753527 |
| 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 | 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 | physiological function |
essential enzyme for the completion of the life cycle of Middle East Respiratory Syndrome Coronavirus |
753344 |
| 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 | physiological function |
the enzyme is required for viral polyprotein processing |
693255 |
