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
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3.4.22.66
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coronavirus
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sars-cov-2
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covid-19
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polyproteins
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pandemic
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repurposing
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outbreak
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plpro
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3-chymotrypsin-like
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papain-like
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rna-dependent
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remdesivir
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ace2
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mers-cov
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ramaswamy
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replicase
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nonstructural
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sarma
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wuhan
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lopinavir
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admet
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anti-sars-cov-2
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mhv-a59
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genogroups
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picornavirus
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caliciviruses
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medicine
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anti-sars
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norwalk
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anti-covid-19
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betacoronavirus
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sars-coronavirus
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anti-coronavirus
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trans-cleavage
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drug development
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pp1ab
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caliciviridae
- 3.4.22.66
- coronavirus
- sars-cov-2
- covid-19
- polyproteins
- pandemic
-
repurposing
-
outbreak
- plpro
-
3-chymotrypsin-like
-
papain-like
-
rna-dependent
- remdesivir
- ace2
- mers-cov
-
ramaswamy
-
replicase
-
nonstructural
-
sarma
-
wuhan
- lopinavir
-
admet
-
anti-sars-cov-2
-
mhv-a59
-
genogroups
- picornavirus
- caliciviruses
- medicine
-
anti-sars
-
norwalk
-
anti-covid-19
- betacoronavirus
-
sars-coronavirus
-
anti-coronavirus
-
trans-cleavage
- drug development
- pp1ab
- caliciviridae
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
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Engineering
Engineering on EC 3.4.22.66 - calicivirin
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E54L
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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
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site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
C139S
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site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
C104S
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site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
C116S
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site-directed mutagenesis, the mutant is affected in its catalytic activity of proteolytic processing
additional information
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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
additional information
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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
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
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