EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.66 | C104S |
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing |
718084 |
| 3.4.22.66 | C116S |
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing |
718084 |
| 3.4.22.66 | C122S |
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing |
718084 |
| 3.4.22.66 | C139A |
cysteine residue responsible for hydrolysis |
671000 |
| 3.4.22.66 | C139S |
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing |
718084 |
| 3.4.22.66 | E54A |
Glu at the active centre |
670097 |
| 3.4.22.66 | E54L |
the E54L mutant protease is a substrate-specificity mutant and requires large hydrophobic amino acid residues at both P4 and P2 positions of the substrate, it cleaves the sequence 133LSFE/AP between the 3B and 3C regions of norovirus polyprotein, but does not cleaves the sequence 198ATSE/GK between the 3A and 3B |
708950 |
| 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 |
