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2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans + H2O
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGG + YIFSE-Edans
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGG + YIFSS-Edans
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGGYI-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGG + YI-Edans
DABCYL-Arg-Ala-Gly-Gly-Tyr-Ile-Phe-Ser-(Glu-EDANS) + H2O
DABCYL-Arg-Ala-Gly-Gly + Tyr-Ile-Phe-Ser-(Glu-EDANS)
-
-
-
?
MBPNusG-His6 p3/p4 + H2O
?
-
-
-
-
?
P123 polyprotein + H2O
?
-
-
-
-
?
P23 polyprotein + H2O
?
-
-
-
-
?
Semliki forest virus p1/p2 + H2O
?
Semliki forest virus p3/p4 + H2O
?
-
-
-
-
?
Sindbis virus core protein + H2O
Hydrolyzed Sindbis core protein
-
-
-
-
?
thioredoxin fusion protein + H2O
?
-
fusion protein is cleaved with greater efficiency by nsp2pro than the original MBP-NusG-His6 substrate with the shorter linker
-
-
?
Venezuelan equine encephalitis virus p1/p2 + H2O
?
-
-
-
?
Venezuelan equine encephalitis virus p3/p4 + H2O
?
-
-
-
?
XJ-160 virus-specific protein + H2O
?
-
-
-
-
?
additional information
?
-
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
-
corresponds to cleavage site P1/2 of the polyprotein
-
-
?
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGA + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
-
corresponds to cleavage site P2/3 of the polyprotein
-
-
?
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGC + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
-
-
-
-
?
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
-
corresponds to cleavage site P3/4 of the polyprotein
-
-
?
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp) + H2O
2-(N-methylamino)benzoyl-AGG + GIIETk(Dnp)
-
-
-
-
?
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans + H2O
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGG + YIFSE-Edans
-
-
-
?
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans + H2O
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGG + YIFSE-Edans
Chikungunya virus S27-African prototype
-
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGG + YIFSS-Edans
-
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGG + YIFSS-Edans
-
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGGYI-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGG + YI-Edans
peptide representing the 1/2 site of the polyprotein. Substrate is processed by nsP2, but the reaction velocity cannot be saturated
-
-
?
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGGYI-Edans + H2O
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-LDRAGG + YI-Edans
peptide representing the 1/2 site of the polyprotein. Substrate is processed by nsP2, but the reaction velocity cannot be saturated
-
-
?
Semliki forest virus p1/p2 + H2O
?
-
-
-
-
?
Semliki forest virus p1/p2 + H2O
?
-
-
-
?
additional information
?
-
-
chikungunya nsP2 protease possesses different substrate specificity to the canonical alphavirus nsP2 polyprotein cleavage specificity
-
-
?
additional information
?
-
protease readily cleaves GFP-10:5-Trx substrates containing short P10-P5' sequences originating from the 1/2 and 3/4 cleavage sites of the polyprotein, but not from the 2/3 site. Enzyme prefers the 3/4 substrate for cleavage in trans
-
-
?
additional information
?
-
protease readily cleaves GFP-10:5-Trx substrates containing short P10-P5' sequences originating from the 1/2 and 3/4 cleavage sites of the polyprotein, but not from the 2/3 site. Enzyme prefers the 3/4 substrate for cleavage in trans
-
-
?
additional information
?
-
-
chikungunya nsP2 protease possesses different substrate specificity to the canonical alphavirus nsP2 polyprotein cleavage specificity
-
-
?
additional information
?
-
-
the catalytic dyad is composed of Cys-481 and His-558
-
-
?
additional information
?
-
-
enzyme is critically involved in development of cytopathic effect. Cytotoxic effect of enzyme is due to its ability to cause transcriptional shutoff
-
-
?
additional information
?
-
-
after negative-strand synthesis, the ns protein appears to irreversibly change conformation and forms mature replication complexes, in spite of the lack of ns polyprotein cleavage. Complete processing of the ns polyprotein is not an absolute prerequisite for Sindbis virus replication. Inability of the viruses with unprocessed polyprotein to productively replicate in the interferon-competent cells and in the cells of mosquito origin is an additional, important factor in ns polyprotein cleavage development. It leads to the release of nsP2 protein, which plays a critical role in inhibiting the cellular antiviral response
-
-
?
additional information
?
-
-
recombinant Sindbis viruses encoding nsP2/GFP chimeric protein are capable of growth in tissue culture and interfering with cellular functions. GFP insertion after the eighth amino acid of nsP2 in the SIN/nsP2GFP/8 virus blocks the processing of one of the cleavage sites. In the SIN/nsP2GFP/472 virus, the GFP insertion causes the formation process for nsP2/GFP to pass through an additional step of processing, in which the intermediate product of a higher molecular weight is initially formed and then processed to a final form of nsP2/GFP
-
-
?
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0.00023 - 0.0364
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
0.00041 - 0.0099
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
0.00016 - 0.009
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
0.01 - 0.029
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
0.0025
4-[[4-(dimethylamino)phenyl]-azo]benzoyl-DELRLDRAGGYIFSS-Edans
30°C, pH not specified in the publication
0.00098
DABCYL-Arg-Ala-Gly-Gly-Tyr-Ile-Phe-Ser-(Glu-EDANS)
pH 8.0, temperature not specified in the publication
0.58 - 1.2
Semliki forest virus p1/p2
-
1.27
Semliki forest virus p3/p4
-
-
-
0.25
Trx34
-
wild-type, at 28°C
-
0.00023
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00033
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00041
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00043
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
pH 7.5, 37°C
0.00104
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00301
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0066
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0093
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.0364
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.00041
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00043
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0007
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.00077
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.00109
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00142
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
pH 7.5, 37°C
0.00184
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0045
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0099
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.00016
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00057
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
pH 7.5, 37°C
0.00058
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.00072
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00076
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00086
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.00269
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0074
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.009
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.01
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
wild-type, pH not specified in the publication, temperature not specified in the publication
0.029
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
mutant N547A, pH not specified in the publication, temperature not specified in the publication
0.58
Semliki forest virus p1/p2
-
-
1.2
Semliki forest virus p1/p2
-
-
-
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0.00052 - 0.0046
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
0.0013 - 0.0075
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
0.00068 - 0.0019
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
0.016 - 0.043
Semliki forest virus p1/p2
-
0.352
Semliki forest virus p3/p4
-
-
-
0.00052
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.00076
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00084
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.00164
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0027
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.00281
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
pH 7.5, 37°C
0.0032
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.0033
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0046
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0013
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.00142
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0021
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0024
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0029
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0031
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0034
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.00445
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
pH 7.5, 37°C
0.0075
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.00068
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
presence of glutathione disulfide, pH 7.5, 37°C
0.0011
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.0013
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.0014
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.0015
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.0016
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.0017
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.00182
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
pH 7.5, 37°C
0.0019
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.016
Semliki forest virus p1/p2
-
-
0.043
Semliki forest virus p1/p2
-
-
-
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0.072 - 0.29
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
0.116 - 0.65
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
0.067 - 0.308
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
0.14 - 0.41
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
0.072
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.091
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.104
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.157
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.164
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.177
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.29
2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.116
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.187
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.242
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.34
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.35
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.361
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.65
2-(N-methylamino)benzoyl-AGCGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.067
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549A, pH 7.5, 37°C
0.15
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
truncated enzyme, pH 7.5, 37°C
0.179
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
wild-type enzyme, pH 7.5, 37°C
0.179
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant W549F, pH 7.5, 37°C
0.21
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
full-length enzyme, pH 7.5, 37°C
0.224
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant C478A, pH 7.5, 37°C
0.308
2-(N-methylamino)benzoyl-AGGGIIETk(Dnp)
-
mutant S482A, pH 7.5, 37°C
0.14
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
mutant N547A, pH not specified in the publication, temperature not specified in the publication
0.41
4-(4-dimethylaminophenyl-azo)benzoyl-DRAGGYIFSE-Edans
wild-type, pH not specified in the publication, temperature not specified in the publication
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N547A
mutation leads to three-fold increase in Km value
W479A
mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
W549A
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
W549F
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
C478A
-
residue Cys478 in the active site of CHIKV nsP2 is indispensable for polyprotein P1234 processing. Mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
-
S482A
-
mutation has almost no negative effect on the protease activity
-
W479A
-
mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
-
C478A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
-
S482A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
-
W549A
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
-
W549F
-
mutation involved in structural stability of the loop that contains the catalytic histidine residue
-
C478A
Chikungunya virus S27-African prototype
-
mutation in active site, loss of activity
-
N547A
Chikungunya virus S27-African prototype
-
mutation leads to three-fold increase in Km value
-
A662T
-
temperature-sensitive in vivo and in vitro
G577R
-
temperature-sensitive in vivo and in vitro
M781T
-
temperature-sensitive in vivo and in vitro
N600D
-
significantly impaired activity. Slower growth rate and smaller bacterial mass as well as a reduced expression level of the corresponding soluble Pro39. Results in preparates with lower degree of purity and shows a tendency to aggregate
N605D
-
significantly impaired activity. Slower growth rate and smaller bacterial mass as well as a reduced expression level of the corresponding soluble Pro39. Results in preparates with lower degree of purity and shows a tendency to aggregate
C481G
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
C481R
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
C481S
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
C525R
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
C525S
-
mutant is active and processed normally
G8063V
-
mutation blocks P2/3 cleavage during P123 processing
H558A
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
H558Q
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
H558Y
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
H619A
-
mutant is active and processed normally
H701A
-
mutant is active and processed normally
H709A
-
mutant is active and processed normally
H709R
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
H709Y
-
mutant is active and processed normally
K173E
-
mutation has any influence on the activity of Sindbis virus nsp2pro
N561D
-
mutant shows some activity, with normal processing
N561S
-
mutant shows some activity, with normal processing
N609D
-
mutant is active, almost no processing
N609S
-
mutant is active, with reduced processing
N614D
-
mutant shows enhanced processing, and is lethal
N614S
-
mutant shows some activity, with normal processing
N693S
-
mutant shows some activity, and is lethal
P726A
-
the mutant exhibits similar growth characteristics to the wild type BR-XJ160 in cultured cells, including cytopathic effects, plaque morphology and growth kinetics
P726L
-
the mutant shows no cytopathic effects or plaques after six passages through BHK-21 cells, although expression of XJ-160 virus-specific protein is detectable, the mutant produces no lethality or morbidity in suckling mice
P726S
-
the mutant shows reduced growth capacity in cultured cells and mouse brain, and intermediate neurovirulence
P726V
-
the mutant exhibits similar growth characteristics to the wild type BR-XJ160 in cultured cells, including cytopathic effects, plaque morphology and growth kinetics
S535T
-
mutant is active and processed normally
Y559A
-
mutation in C-terminal protease domain, abolishes catalytic activity, and is lethal
G17V
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
K480A
mutation leads to a 9fold decrease in kcat and kcat/Km. K480 likely enhances the nucleophilicity of the Cys residue
K706A
SAM MTase domain mutation, increases Km 4.5fold to 500 microM
N545A
mutation within the beta-hairpin, lightly but not significantly increases kcat and Km
N545D
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
Q471L
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
R662A
mutation leads to 16fold decreases in kcat/Km
R662K
mutation leads to 16fold decreases in kcat/Km
S701A
mutation leads to a 17fold increase in Km
T5A
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
T5I
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
V3A
-
mutation causes an increase in infectous viral titer, variants become cytopathic for both BHK-21 and Vero cells
K480A
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation leads to a 9fold decrease in kcat and kcat/Km. K480 likely enhances the nucleophilicity of the Cys residue
-
K706A
Venezuelan equine encephalitis virus Trinidad donkey
-
SAM MTase domain mutation, increases Km 4.5fold to 500 microM
-
R662A
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation leads to 16fold decreases in kcat/Km
-
R662K
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation leads to 16fold decreases in kcat/Km
-
S701A
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation leads to a 17fold increase in Km
-
C478A
complete loss of activity
C478A
mutation in active site, loss of activity
C478A
residue Cys478 in the active site of CHIKV nsP2 is indispensable for polyprotein P1234 processing. Mutation completely abolishes RNA replication trans-replication systems and abolishes the rescue of infectious virus from CHIKV RNA transcripts
C478A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
S482A
mutation has almost no negative effect on the protease activity
S482A
-
significantly less activity than wild type for the 2-(N-methylamino)benzoyl-AGAGIIETk(Dnp)substrate
N475A
mutation leads to a 24fold reduction in kcat/Km, and the conformation of this residue does not change after inhibition. Residue N475 forms the base of the P1 binding site and likely orients the substrate for nucleophilic attack or plays a role in product release
N475A
mutation of a conserved motif residue, produces a self-inhibited state in which the N-terminal residues flipp into the substrate-binding cleft. Mutation results in a 70fold decrease in kcat/Km
N475A
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation leads to a 24fold reduction in kcat/Km, and the conformation of this residue does not change after inhibition. Residue N475 forms the base of the P1 binding site and likely orients the substrate for nucleophilic attack or plays a role in product release
-
N475A
Venezuelan equine encephalitis virus Trinidad donkey
-
mutation of a conserved motif residue, produces a self-inhibited state in which the N-terminal residues flipp into the substrate-binding cleft. Mutation results in a 70fold decrease in kcat/Km
-
additional information
-
preparation of both full length and a truncated protease domain from the C-terminus of the nsP2 protein. The protease domain alone has different properties compared with the full length nsP2 protease
additional information
-
preparation of both full length and a truncated protease domain from the C-terminus of the nsP2 protein. The protease domain alone has different properties compared with the full length nsP2 protease
-
additional information
-
mutants with deletions and/or mutations at the N-terminal border of the nsp2 PLP2-DUB domain. A 23-amino-acid deletion of amino acids 402 to 424 of the ORF1a-encoded protein largely abolishes the inhibitory effect of nsp2 on ubiquitin-like protein ISG15 production and conjugation, but no viable recombinant virus is recovered. A 19-amino-acid deletion of amino acids 402 to 420, in combination with downstream point mutation S465A, partially relieves the ISG15 antagonist function and yields a viable recombinant virus
additional information
-
SIN/2V/389 virus, has GFP insertion after aa 389 of nsP3 and a single-point mutation leading to replacement of glycine by valine in the P2 position of the cleavage site between nsP2 and nsP3. Blocks polyprotein processing
additional information
-
ns polyprotein cleavage mutants of Sindbis virus differ from the Sindbis virus/GFP variant in their ability to inhibit cellular translation and transcription. The nsP2/nsP3 cleavage site mutant replicates in BHK-21 cells almost as efficiently as the cleavage competent Sindbis virus/GFP. In the case of the 1V2V ns polyprotein mutant, only one additional substitution in the nsP4 protein sequence is required to strongly increase RNA replication (but not the transcription of the subgenomic RNA) to the wild-type level. Ns polyprotein cleavage mutants induce a strong interferon-alpha/beta response
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Identification of the active site residues in the nsP2 proteinase of Sindbis virus
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Homology modeling, molecular dynamics, e-pharmacophore mapping and docking study of Chikungunya virus nsP2 protease
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Sindbis virus, Semliki forest virus (P08411), Chikungunya virus (Q8JUX6), Chikungunya virus
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Kinetic, mutational, and structural studies of the Venezuelan equine encephalitis virus nonstructural protein 2 cysteine protease
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Mutation of Asn-475 in the Venezuelan equine encephalitis virus nsP2 cysteine protease leads to a self-inhibited state
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Glutathionylation of chikungunya nsP2 protein affects protease activity
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Chikungunya virus (C8YZ72), Chikungunya virus, Chikungunya virus 899 (C8YZ72)
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Structure-function relationship of Chikungunya nsP2 protease A comparative study with papain
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Crystal structure of chikungunya virus nsP2 cysteine protease reveals a putative flexible loop blocking its active site
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