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Literature summary for 3.4.22.66 extracted from

  • Oka, T.; Murakami, K.; Wakita, T.; Katayama, K.
    Comparative site-directed mutagenesis in the catalytic amino acid triad in Calicivirus proteases (2011), Microbiol. Immunol., 55, 108-114.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C104S site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing Rabbit hemorrhagic disease virus
C116S site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing Sapporo virus
C122S site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing feline calicivirus
C139S site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing Norwalk virus
additional information 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 Rabbit hemorrhagic disease virus
additional information 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 Norwalk virus
additional information 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 feline calicivirus
additional information 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 Sapporo virus

Organism

Organism UniProt Comment Textmining
feline calicivirus
-
FCV
-
Norwalk virus
-
NoV
-
Rabbit hemorrhagic disease virus
-
RHDV
-
Sapporo virus
-
SaV
-

Synonyms

Synonyms Comment Organism
calicivirus protease
-
Rabbit hemorrhagic disease virus
calicivirus protease
-
Norwalk virus
calicivirus protease
-
feline calicivirus
calicivirus protease
-
Sapporo virus

General Information

General Information Comment Organism
additional information 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 Rabbit hemorrhagic disease virus
additional information 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 Norwalk virus
additional information 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 feline calicivirus
additional information 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 Sapporo virus
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 Rabbit hemorrhagic disease virus
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 Sapporo virus
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 feline calicivirus
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 Norwalk virus