EC Number   |
Natural Substrates |
|---|
   3.4.21.113 | bovine viral diarrhea virus polyprotein + H2O |
the enzyme is required for pestivirus replication. The enzyme is required for processing at nonstructural protein sites 3/4A, 4A/4B, 4B/5A and 5A/5B but not for cleavage at the junction between NS2 and NS3. A conserved Leu is found at the P1 position of all four cleavage sites, followed by either Ser (3/4A, 4B5A, and 5A/5B sites) or Ala (4A/4B site) at the P1' position |
| 3.4.21.113 | bovine viral diarrhea virus polyprotein + H2O |
pestivirus P80 protein is a viral proteinase responsible for nonstructural polyprotein cleavage events |
| 3.4.21.113 | DPNRKRGWPA + H2O |
- |
| 3.4.21.113 | DSSTKRGGSW + H2O |
preferred substrate, 33.5% cleavage, the active protease is able to cleave the substrate at the endoplasmic reticulum membrane in Huh-7 cells |
| 3.4.21.113 | FASGKRSQIG + H2O |
- |
| 3.4.21.113 | KPGLKRGGAK + H2O |
preferred substrate, 34.5% cleavage |
| 3.4.21.113 | LQYTKRGGVL + H2O |
- |
| 3.4.21.113 | more |
the NS3 protease of West nile virus has a cleavage sequence preference of (K/R)R-GG |
| 3.4.21.113 | more |
autocatalytic intramolecular cleavages of the enzyme, overview. Intramolecular cleavage of the peptide bond occurs between Leu1781 and Met1782 is required for activity, but cleavage of the Leu1748/Lys1749 peptide bond yields a proteolytically inactive NS3 fragment |
| 3.4.21.113 | more |
pestiviral NS3 is a multifunctional molecule possessing protease, NTPase, and helicase activity |
