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Literature summary for 3.4.22.69 extracted from

  • Shi, J.; Song, J.
    The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain (2006), FEBS J., 273, 1035-1045.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant glutathione S-transferase-fusion constructs are transformed into Escherichia coli BL21 cell strain for overexpression Severe acute respiratory syndrome-related coronavirus

Protein Variants

Protein Variants Comment Organism
C300A mutant enzyme shows more than 30% of wild-type activity Severe acute respiratory syndrome-related coronavirus
E288A mutant enzyme retains less than 10% of the wild-type activity Severe acute respiratory syndrome-related coronavirus
F291A activity is higher than that of wild-type enzyme Severe acute respiratory syndrome-related coronavirus
G283A no significant activity differences from the wild-type protease Severe acute respiratory syndrome-related coronavirus
I286A activity is higher than that of wild-type enzyme Severe acute respiratory syndrome-related coronavirus
L282A mutant enzyme shows more than 30% of wild-type activity Severe acute respiratory syndrome-related coronavirus
N214A mutant enzyme shows more than 30% of wild-type activity Severe acute respiratory syndrome-related coronavirus
N289A mutant enzyme retains less than 10% of the wild-type activity Severe acute respiratory syndrome-related coronavirus
Q290A mutant enzyme retains less than 10% of the wild-type activity Severe acute respiratory syndrome-related coronavirus
Q299A mutant enzyme retains less than 10% of the wild-type activity Severe acute respiratory syndrome-related coronavirus
R298A mutant enzyme retains less than 10% of the wild-type activity Severe acute respiratory syndrome-related coronavirus
S284A activity is higher than that of wild-type enzyme Severe acute respiratory syndrome-related coronavirus
S284A/T285A/I286A activity is 3.7fold higher than wild-type activity Severe acute respiratory syndrome-related coronavirus
S301A no significant activity differences from the wild-type protease Severe acute respiratory syndrome-related coronavirus
T280A no significant activity differences from the wild-type protease Severe acute respiratory syndrome-related coronavirus
T285A activity is higher than that of wild-type enzyme Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[4-(4-dimethylaminophenylazo)benzoic acid]-KTSAVLQSGF RKME-[5-[2'-(aminoethyl)amino]-naphthalenesulfonic acid] + H2O
-
Severe acute respiratory syndrome-related coronavirus ?
-
?

Synonyms

Synonyms Comment Organism
SARS 3C-like protease
-
Severe acute respiratory syndrome-related coronavirus