EC Number   |
General Information |
Reference |
|---|
   3.4.22.66 | drug target |
the enzyme is an attractive target for the discovery of norovirus therapeutics and prophylactics. In order to gain insight and understanding into the interaction of macrocyclic inhibitors with the enzyme, as well as probe the effect of ring size on pharmacological activity and cellular permeability, additional macrocyclic inhibitors are synthesized and high resolution cocrystal structures determined. The macrocyclic scaffold may hamper optimal binding to the active site by impeding concerted cross-talk between the S2 and S4 subsites |
-, 755356 |
| 3.4.22.66 | more |
acidic amino acid (Glu or Asp), as well as the His and Cys in the putative catalytic triad, cannot be replaced by Ala for normal processing activity of the ORF1 polyprotein in vitro. Similarly, normal activity is not retained if the nucleophile Cys is replaced with Ser |
718084 |
| 3.4.22.66 | physiological function |
noroviruses have a single-stranded, positive sense 7 to 8 kb RNA genome which encodes a polyprotein precursor that is processed by a virus-encoded 3C-like cysteine protease (NV 3CLpro) to generate at least six mature nonstructural proteins. Processing of the polyprotein is essential for virus replication |
-, 755356 |
| 3.4.22.66 | physiological function |
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys104, and the His27-Asp44-Cys104 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. RHDV protease critically needs the acidic residue during catalysis |
718084 |
| 3.4.22.66 | physiological function |
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys116, and the His31-Glu52-Cys116 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. SaV protease critically needs the acidic residue during catalysis |
718084 |
| 3.4.22.66 | physiological function |
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys122, and the His39-Glu60-Cys122 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the FCV protease |
718084 |
| 3.4.22.66 | physiological function |
the Calicivirus proteases cleaves the viral precursor polyprotein encoded by open reading frame1 into multiple intermediate and mature proteins. The Calicivirus protease is a Cys protease with catalytic Cys139, and the His30-Glu54-Cys139 catalytic triad formation is important for protease activity. The substrate recognition mechanism may be different between Caliciviridae, i.e. the Rabbit hemorrhagic disease virus and Sapporo virus proteases and the Norwalk virus and Feline calicivirus proteases. Proteolytic cleavage occurs at several cleavage sites in the ORF1 polyprotein without a functional acid residue in the NoV protease |
718084 |
| 3.4.22.66 | physiological function |
the enzyme is required for viral polyprotein processing |
693255 |
| 3.4.22.66 | physiological function |
the feline calicivirus strain 2280 proteinase-polymerase protein can suppress luciferase reporter gene expression driven by endogenous and exogenous promoters. The N-terminal 263 amino acids of proteinase-polymerase (PPN-263) determine its shut-off activity upon the expression of truncated proteins. The same domain of the feline calicivirus strain F9 proteionase-polymeraseprotein fails to inhibit gene expression. Residues Val27, Ala96 and Ala98 are key sites for the inhibition of host gene expression by strain 2280 PPN-263, and PPN-263 exhibits the ability to shut off host gene expression as long as it contains any two of the three amino acids |
-, 755657 |
