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3.4.22.66: calicivirin

This is an abbreviated version!
For detailed information about calicivirin, go to the full flat file.

Word Map on EC 3.4.22.66

Reaction

endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-/- and the P1' position is occupied by Gly-/- =

Synonyms

3C protease, 3C-like cysteine protease, 3C-like protease, 3C-like proteinase, 3C-like viral protease, 3CL Pro, 3cLpro, 3CP, 3Cpro, C37.001, calicivirus protease, CVP, FCV 3CLpro, NoV 3CLpro, NV 3CLpro, NV protease, NVPro, Pro, PV 3Cpro, Southampton virus 3C-like protease, viral cysteine protease, virus-encoded 3C-like proteinase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.66 calicivirin

Engineering

Engineering on EC 3.4.22.66 - calicivirin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C139A
-
cysteine residue responsible for hydrolysis
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
C122S
-
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
C139S
-
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
E54A
Glu at the active centre
C104S
-
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
C116S
-
site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
additional information