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1C'D2A precursor polypeptide + H2O
?
-
i.e. autocatalytic cis cleavage activity, cleaves at 1D/2A junction in very rapid cotranslational reaction
-
-
?
2-aminobenzoic acid-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Phe(NO2)-Ala-OH + H2O
?
-
-
-
-
?
3CD-precursor poliovirus protein + H2O
poliovirus 3C' and 3D'-protein
-
-
-
?
acetyl-LSTT-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-LSTT + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Arg-Arg-Asn-Thr-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Arg-Arg-Asn-Thr-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein, poor substrate
-
?
Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P7-P8', hydrolyzed with about the same relative efficiency compared to P8-P8'
-
?
Bid protein + H2O
?
-
-
-
-
?
cAMP-regulated response element binding protein + H2O
?
-
-
-
-
?
capsid precursor protein P1 + H2O
viral protein 1ABC + viral protein 1D
-
-
-
?
cellular eukaryotic translation initiation factor 4G + H2O
?
cellular eukaryotic translation initiation factor eIF4GI + H2O
peptides
-
-
-
-
?
cellular eukaryotic translation initiation factor eIF4GII + H2O
peptides
-
-
-
-
?
CVB1 protein + H2O
?
-
-
-
-
?
death-associated protein 5 + H2O
?
DIKSYGLGPRYGG + H2O
DIKSY + GLGPRYGG
-
-
-
-
?
eIF4G + H2O
fragments of eIF4G
-
-
-
-
?
eIF4GI + H2O
fragments of eIF4GI
-
-
-
-
?
eukaryotic initiation factor 4G + H2O
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
eukaryotic translation initiation factor 4G + H2O
?
eukaryotic translation initiation factor 4G I + H2O
?
-
-
-
?
eukaryotic translation initiation factor 4G II + H2O
?
-
-
-
?
eukaryotic translation initiation factor 4gamma + H2O
?
-
-
-
-
?
eukaryotic translation initiation factor 4Gl + H2O
?
-
-
-
-
?
EV-A71 viral polyprotein + H2O
?
Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Glu-Arg-Ala-Ser-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein
-
?
Glu-Arg-Ala-Ser-Leu-Ile-Thr-Thr-Gly-Pro-Tyr-Gly-His-Gln-Ser-Gly + H2O
Glu-Arg-Ala-Ser-Leu-Ile-Thr-Thr-Gly-Pro-Tyr + Gly-His-Gln-Ser-Gly
-
-
-
-
?
Gly-Leu-Gly-Gln-Met methyl ester + H2O
Gly-Leu-Gly-Gln-Met + CH3OH
-
esterase activity
-
?
Grb2-associated binding protein 1 + H2O
?
-
GAB1 is cleaved during CV-B3 infection by viral proteinase 2A
-
-
?
Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
GRTTLST-(3-nitrotyrosine)-GPPR-(lysine anthranilide)-Y + H2O
GRTTLST-(3-nitrotyrosine) + GPPR-(lysine anthranilide)-Y
-
-
-
-
?
HRV 3Cpro precursor 3CD + H2O
3Cpro + 3Dpro
-
activation of 3C protease, EC 3.4.22.28, of human rhinovirus A-16
-
-
?
human eukaryotic translation initiation factor 4 G I + H2O
?
human eIF4GI
-
-
?
human eukaryotic translation initiation factor 4 G II + H2O
?
human eIF4GII
-
-
?
Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P5-P8', poor substrate
-
?
Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P4-P8', poor substrate
-
?
KSYKVSTSGPRAFSSR + H2O
KSYKVSTS + GPRAFSSR
L-Leu-Val-Pro-Arg-Gly-Ser + H2O
L-Leu-Val-Pro-Arg + Gly-Ser
-
-
-
-
?
modified pentadecameric peptides + H2O
?
-
i.e. synthetic P8-P7' peptides, intermolecular specificity, changes at P2 and P1' are highly deleterious
-
-
?
mouse double minute 2 + H2O
?
-
-
-
-
?
mouse double minute 4 + H2O
?
-
-
-
-
?
nuclear factor of activated T cells 5/tonicity enhancer binding protein
?
oligopeptides corresponding to cleavage sites of coxsackievirus + H2O
?
-
-
-
-
?
oligopeptides corresponding to cleavage sites of human rhinovirus + H2O
?
-
-
-
-
?
oligopeptides corresponding to cleavage sites of poliovirus type 1 + H2O
?
oligopeptides derived from eIF-4gamma + H2O
?
-
human rhinovirus, common cleavage site: Ala-Gly
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
picornavirus polyprotein + H2O
?
-
intramolecular reaction, processing begins before synthesis of the polyprotein is complete, cleavage separates capsid protein precursor and noncapsid protein precursor
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
poliovirus polypeptide + H2O
?
poliovirus polyprotein fragment + H2O
hydrolyzed poliovirus polyprotein fragment
-
containing cleavage site at P1/P2 junction
partially cleaved in trans
?
poly(A) binding protein + H2O
fragments of poly(A) binding protein
-
contains 1 cleavage site for 2A proteinase within the proline-rich linker domain
-
-
?
poly-(ADP-ribose) polymerase + H2O
?
-
-
-
-
?
polyadenylate-binding protein 1 + H2O
?
Pro-Arg-Ala-Ser-Met-Lys-Thr-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Arg-Ala-Ser-Met-Lys-Thr-Val + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
poor substrate
-
?
Pro-Arg-Glu-Asn-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Arg-Glu-Asn-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein, poor substrate
-
?
pro-caspase 3 + H2O
caspase 3 + ?
-
-
-
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
i.e. synthetic peptide P6-P5', hydrolyzed with 42% relative efficiency compared to P8-P8'
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
-
i.e. synthetic peptide P6-P6', hydrolyzed with 45% relative efficiency compared to P8-P8', smallest cleavable symmetric peptide
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
i.e. synthetic peptide P6-P7', hydrolyzed with 55% relative efficiency compared to P8-P8'
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
RKGDIKS-(3-nitrotyrosine)-GPGP-(lysine-anthranilide)-Y + H2O
RKGDIKS-(3-nitrotyrosine) + GPGP-(lysine-anthranilide)-Y
-
-
-
-
?
RKGDIKSY-p-nitroanilide + H2O
RKGDIKSY + p-nitroaniline
-
-
-
-
?
RKGDIKSYG + H2O
RKGDIKSY + glycine
-
-
-
-
?
RKGDIKSYGLGPR + H2O
RKGDIKSY + GLGPR
-
-
-
-
?
RKGDIKSYGLGPRYGG + H2O
RKGDIKSY + GLGPRYGG
-
-
-
-
?
RKGDIKT-(3-nitrotyrosine)-GPGP-(lysine-anthranilide)-Y + H2O
RKGDIKT-(3-nitrotyrosine) + GPGP-(lysine-anthranilide)-Y
-
-
-
-
?
Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Ser-Arg-Ala-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
peptide derived from poliovirus type 1 polyprotein
-
?
Ser-Thr-Lys-Asn-Leu-Thr-Thr-Gly-Phe-Gly-His-Gln-Asn-Lys-Ala + H2O
Ser-Thr-Lys-Asn-Leu-Thr-Thr-Tyr + Gly-Phe-Gly-His-Gln-Asn-Lys-Ala
-
synthetic hexadecapeptide corresponding to P1/P2 junction
-
?
Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr-Gly-Phe-Gly-His-Gln-Asn-Lys-Ala + H2O
Ser-Thr-Lys-Asp-Ile-Thr-Thr-Tyr + Glys-Phe-Gly-His-Gln-Asn-Lys-Ala
-
poor substrate
-
?
serum response factor + H2O
?
-
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + glycine
-
i.e. synthetic peptide P8-P1', poor substrate, smallest cleavable asymmetric peptide
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro
-
i.e. synthetic peptide P8-P2', hydrolyzed with about the same relative efficiency as P8-P8'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp
-
i.e. peptide P8-P4'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met
-
i.e. peptide P8-P5'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr
-
i.e. synthetic peptide P8-6'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val
-
i.e. synthetic peptide P8-7'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Val-Tyr + H2O
?
-
-
-
-
?
TRPIITT-(3-nitrotyrosine)-GPSD-(lysine-anthranilate)-Y + H2O
TRPIITT-(3-nitrotyrosine) + GPSD-(lysine-anthranilate)-Y
-
-
-
-
?
TRPIITTA-p-nitroanilide + H2O
TRPIITTA + p-nitroaniline
-
-
-
-
?
TRPIITTAGPSDMYV + H2O
TRPIITTA + GPSDMYV
-
-
-
-
?
additional information
?
-
cellular eukaryotic translation initiation factor 4G + H2O
?
-
-
-
-
?
cellular eukaryotic translation initiation factor 4G + H2O
?
-
eIF4GI, trans-cleavage
-
-
?
cytokeratin 8 + H2O
?
-
-
-
-
?
cytokeratin 8 + H2O
?
-
the cleavage results in removal of 14 amino acids from the N-terminal head domain of cytokeratin 8
-
-
?
cytokeratin 8 + H2O
?
-
the cleavage results in removal of 14 amino acids from the N-terminal head domain of cytokeratin 8. Cleavage occurs late in the infection cycle at the time of the onset of the cytopathic effect
-
-
?
death-associated protein 5 + H2O
?
-
DAP5
-
-
?
death-associated protein 5 + H2O
?
-
DAP5, generation of 45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments, respectively. DAP5 is cleaved at amino acid G434
-
-
?
dystrophin + H2O
?
-
human dystrophin is cleaved between residue 588 and 589 and between residue 2434 and 2435. Rat dystrophin is cleaved between resiue 590 and 591 and between residue 2427 and 2428
-
-
?
dystrophin + H2O
?
-
cleavage of mouse dystrophin at residue 2427 and human dystrophin at residue 2434
-
-
?
dystrophin + H2O
?
-
the protease cleaves dystrophin in coxsackievirus B3-infected myocytes. The cleavage functionally impairs dystrophin
-
-
?
dystrophin + H2O
?
-
functional impairment and morphological disruption of dystrophin
-
-
?
dystrophin + H2O
?
-
-
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eIF4G + H2O
?
-
eukaryotic initiation factor-4G
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eIF4G + H2O
?
-
recombinant enzyme cleaves either rabbit or human eIF4G or their derived peptides, cleaves the 4G-derived peptides with 100fold lower efficiency than with a peptide derived from the poliovirus polyprotein. Up to 25fold molar excess of the enzyme over eIF4G protein is required to cause greater than 50% cleavage
-
-
?
eIF4G + H2O
?
-
efficient cleavage
-
-
?
eIF4G + H2O
?
-
self-processing is prerequisite for eIF4GI cleavage
-
-
?
eIF4G + H2O
?
-
cleavage reactions utilizing recombinant eIF4G containing a G486E substitution at the cleavage site results in drastically reduced clevage activity
-
-
?
eIF4G + H2O
?
-
cleavage site: PLLNV699-/-GSR
-
-
?
eukaryotic initiation factor 4G + H2O
?
-
-
-
?
eukaryotic initiation factor 4G + H2O
?
-
-
-
?
eukaryotic initiation factor 4G + H2O
?
-
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
involved in shut-off in translation of cellular mRNAs upon viral infection, induces cleavage of eukaryotic initiation factor (eIF)4gamma component (i.e. p220) of eIF-4, formerly eIF-4F
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
?
-
turns off host-cell protein synthesis
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
-
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vitro
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
mapping of cleavage site
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
i.e. (eIF)-4Fgamma
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from HeLa cell extracts
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from rabbit
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
cleavage site: Arg486-Gly (rabbit), Arg485-Gly (human)
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vivo
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in-trans activity
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vitro
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
mapping of cleavage site
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
i.e. (eIF)-4Fgamma
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from HeLa cell extracts
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
from rabbit
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
cleavage site: Arg486-Gly (rabbit), Arg485-Gly (human)
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
in vivo
-
-
?
eukaryotic translation initiation factor 4F p220 subunit + H2O
protein CPa + protein CPb
-
the 2Apro cleavage site on eIF4GI is TLSTR*GPPR
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
-
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
-
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
-
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
Enterovirus A71 BrCR
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
-
eIF4G
-
-
?
eukaryotic translation initiation factor 4G + H2O
?
eIF4G
-
-
?
EV-A71 viral polyprotein + H2O
?
-
-
-
-
?
EV-A71 viral polyprotein + H2O
?
-
cis-cleavage
-
-
?
Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
-
GAB2 is cleaved at G238 during CV-B3 infection by viral proteinase 2A, generating two cleaved fragments of GAB2-N1-237 and GAB2-C238-676
-
-
?
Grb2-associated binding protein 2 + H2O
GAB2-N1-237 + GAB2-C238-676
-
GAB2 is cleaved at G238 during CV-B3 infection by viral proteinase 2A, generating two cleaved fragments of GAB2-N1-237 and GAB2-C238-676. mutant GAB2G238E is non-cleavable for the enzyme
-
-
?
KSYKVSTSGPRAFSSR + H2O
KSYKVSTS + GPRAFSSR
-
-
-
-
?
KSYKVSTSGPRAFSSR + H2O
KSYKVSTS + GPRAFSSR
-
-
-
-
?
MAVS + H2O
?
-
a cellular protein
-
-
?
MAVS + H2O
?
-
a cellular protein
-
-
?
MAVS + H2O
?
-
a cellular protein
-
-
?
MAVS + H2O
?
-
a cellular protein
-
-
?
MDA5 + H2O
?
-
a cellular protein
-
-
?
MDA5 + H2O
?
-
a cellular protein
-
-
?
MDA5 + H2O
?
-
a cellular protein
-
-
?
MDA5 + H2O
?
-
a cellular protein
-
-
?
nuclear factor of activated T cells 5/tonicity enhancer binding protein
?
-
NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, inactivation of NFAT5
-
-
?
nuclear factor of activated T cells 5/tonicity enhancer binding protein
?
-
NFAT5/TonEBP, a cellular transcription factor, the protein is cleaved by CVB3 protease 2A at Gly503, which is the only CVB3 protease 2A cleavage site on NFAT5, leading to inactivation of NFAT5
-
-
?
oligopeptides corresponding to cleavage sites of poliovirus type 1 + H2O
?
-
-
-
-
?
oligopeptides corresponding to cleavage sites of poliovirus type 1 + H2O
?
-
-
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from poliovirus
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from rhinovirus, cleaves P1/P2 junction
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from poliovirus
-
-
?
P1/P2 precursor polypeptide + H2O
poliovirus 1C'D polypeptide + proteinase 2Apro
-
from rhinovirus, cleaves P1/P2 junction
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage between C-terminus of VP1 and N-terminus of picornain 2A
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage between C-terminus of VP1 and N-terminus of picornain 2A
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage between C-terminus of VP1 and N-terminus of picornain 2A
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
-
-
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage between C-terminus of VP1 and N-terminus of picornain 2A
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
immediately after protease 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent rhinovirus or enterovirus chain is cleaved intramolecularly
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleavage between C-terminus of VP1 and N-terminus of picornain 2A
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves intermolecularly at a second site in the 3D protein between 3C' and 3D'
-
?
picornavirus polyprotein + H2O
hydrolyzed picornavirus polyprotein
-
cleaves Tyr-Gly pairs in both Thr-Tyr-Gly sequences of poliovirus polyprotein, cleaves Thr-Gly in Thr-Thr-Gly (serotype B1) or Asn-Thr-Gly (serotype B3) of coxsackievirus polyprotein, cleaves Ala-Gly in Thr-Ala-Gly (HRV 2), Tyr-Gly in Ser-Tyr-Gly (HRV 14) and Val-Gly in Asn-Val-Gly (HRV 89) in rhinovirus polyproteins
-
?
poliovirus polypeptide + H2O
?
-
involved in primary processing of poliovirus
-
-
?
poliovirus polypeptide + H2O
?
-
involved in primary processing of poliovirus
-
-
?
poliovirus polypeptide + H2O
?
-
involved in primary processing of poliovirus
-
-
?
poliovirus polypeptide + H2O
?
-
immediately after polypeptide 2A has been synthesized the Tyr-Gly pair between P1 and P2 of the nascent chain is cleaved intramolecularly
-
-
?
poliovirus polypeptide + H2O
?
-
together with 3C protease
-
-
?
poliovirus polypeptide + H2O
?
-
involved in primary processing of poliovirus
-
-
?
polyadenylate-binding protein 1 + H2O
?
PABP
-
-
?
polyadenylate-binding protein 1 + H2O
?
Enterovirus A71 BrCR
PABP
-
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P6-P8'
-
?
Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
hydrolyzed with 70% relative efficiency compared to P8-P8'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
-
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
i.e. synthetic peptide P8-P8'
-
?
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Asp-Met-Tyr-Val-His + H2O
Thr-Arg-Pro-Ile-Ile-Thr-Thr-Ala + Gly-Pro-Ser-Asp-Met-Tyr-Val-His
-
best substrate for rhinovirus enzyme
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
no hydrolysis of some modified pentadecameric synthetic peptides P8-P7'(overview), synthetic peptides P3-P8', Arg-Lys-Gly-Asp-Ile-Lys-Ser-Tyr-Gly-Ile-Gly-Pro-Arg-Tyr-Gly-Gly, Asn-Val-Arg-Ala-Val-Lys-Asn-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His, Asp-Val-Phe-Thr-Asn-Val-Gly-Pro-Ser-Ser-Met-Phe-Val-His
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
-
fusion of the C-terminal three amino acid residues of VP1 to the N-terminus of 2Apro is necessary for specific self-cleavage activity to generate mature 2Apro
-
-
?
additional information
?
-
-
2Apro cleaves eIF4G, separating the domains of eIF4GI or eIF4GII that bind to eIF4E (and mRNA) and eIF3 (and the 40S ribosome) and inhibits de novo translation initiation by interfering with the ribosome mRNA binding step
-
-
?
additional information
?
-
-
does not cleave death-associated protein 5
-
-
?
additional information
?
-
-
DAP5 is cleaved during CVB3 infection in tissue culture and in mouse heart
-
-
?
additional information
?
-
-
in vivo assays by expression of GAB2 proteins in virus-infected HeLa cells
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
no activity with mutant substrates PABPM490P/Q540N and eIF4GIG689E
-
-
?
additional information
?
-
-
no activity with mutant substrates PABPM490P/Q540N and eIF4GIG689E
-
-
?
additional information
?
-
Enterovirus A71 BrCR
no activity with mutant substrates PABPM490P/Q540N and eIF4GIG689E
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
no cleavage by single-site mutant enzymes with substitutions at Cys55, Cys57, Cys115 or His117
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
-
enzyme, or its polyprotein precursors, are required to stabilize viral RNA and prolong translation. Enzyme activity stimulates negative-strand initiation by approximately fivefold, but has no effect on stability. Stimulation of negative-strand synthesis is independent of the effect on stability and translation
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
-
2A proteinase of human rhinovirus cleaves the virally encoded polyprotein (-Ile-Ile-Thr-Thr-Ala*Gly-Pro-Ser-Asp-) between the C terminus of VP1 and its own N terminus
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
the enzyme displays a charged aspartic acid, which may significantly influence the interaction between the thiol and imidazole groups
-
-
?
additional information
?
-
-
no hydrolysis of some modified pentadecameric synthetic peptides P8-P7'(overview), synthetic peptides P3-P8', Arg-Lys-Gly-Asp-Ile-Lys-Ser-Tyr-Gly-Ile-Gly-Pro-Arg-Tyr-Gly-Gly, Asn-Val-Arg-Ala-Val-Lys-Asn-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His, Asp-Val-Phe-Thr-Asn-Val-Gly-Pro-Ser-Ser-Met-Phe-Val-His
-
-
?
additional information
?
-
-
no hydrolysis of some modified pentadecameric synthetic peptides P8-P7'(overview), synthetic peptides P3-P8', Arg-Lys-Gly-Asp-Ile-Lys-Ser-Tyr-Gly-Ile-Gly-Pro-Arg-Tyr-Gly-Gly, Asn-Val-Arg-Ala-Val-Lys-Asn-Val-Gly-Pro-Ser-Asp-Met-Tyr-Val-His, Asp-Val-Phe-Thr-Asn-Val-Gly-Pro-Ser-Ser-Met-Phe-Val-His
-
-
?
additional information
?
-
-
synthetic peptides with replacements of P1 or P1' residues with epsilon-amino caproic acid or statine
-
-
?
additional information
?
-
-
residues Gly123, Gly124, Thr121 and Cys101 are proposed to be involved in the architecture of the substrate binding pocket and to provide the correct environment for the catalytic triad of His18, Asp35, and Cys106. Residues Tyr85 and Tyr86 are thought to participate in substrate recognition
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
-
the active site of the enzyme consists of a catalytic triad formed by His18, Asp35 and Cys106
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
the primary cleavage in cardio- and aphthovirus occurs between 2A and 2B (cleavage site: Gly-Pro in-Asn-Pro-Gly-Pro-)
-
-
?
additional information
?
-
-
enzyme is active both as structural element of a precursor and as mature protein
-
-
?
additional information
?
-
-
2Apro processes the viral polyprotein, and it cleaves a variety of host proteins, including the translation proteins eIF4GI, eIF4GII and poly(A)-binding protein
-
-
?
additional information
?
-
-
important cellular substrate for 2Apro is eIF4G, cleavage of this translation protein leads to inhibition of host protein synthesis during picornavirus infection
-
-
?
additional information
?
-
-
inhibitory role for 2Apro in the most downstream event in interferon signaling, the antiviral activities of interferon-stimulated genes
-
-
?
additional information
?
-
-
picornaviral 2A sequences are used to express transgenes in oncolytic adenoviruses
-
-
?
additional information
?
-
-
proteinase 2Apro is essential for enterovirus replication in type I interferon-treated cells
-
-
?
additional information
?
-
-
ribosome skipping is a mechanism that allows translation of multiple proteins from a single mRNA, it is based on the use of a picornaviral 2A sequence that causes the ribosome to continue translation after skipping the formation of one peptide bond
-
-
?
additional information
?
-
-
2A proteinase of human rhinovirus cleaves the virally encoded polyprotein (-Ile-Ile-Thr-Thr-Ala*Gly-Pro-Ser-Asp-) between the C terminus of VP1 and its own N terminus
-
-
?
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metabolism
-
regulation of enterovirus 2A protease-associated viral IRES activities by the cell's ERK signaling cascade. The positive regulation of virus replication by the ERK cascade is mediated through effects on both the cis-cleavage of the viral polyprotein by 2Apro and its trans-cleavage of cellular eIF4GI. The ERK cascade positively regulates EV-A71-mediated cleavage of eIF4GI that establishes the cellular conditions which favour vIRES-dependent translation. This ERK-2Apro linked network coordinating vIRES efficiency is also found in other important human enteroviruses
malfunction
-
a PV 2Apro variant deficient in eukaryotic initiation factor (eIF) 4GI cleavage does not increase picornavirus IRES-driven translation
malfunction
-
a catalytic mutant of 2A (2Amut) fails to cleave GAB2. Deletion of GAB1 causes a decrease in phosphorylated ERK1/2, but knockdown of GAB2 has no effect on virus-mediated ERK1/2 phosphorylation
malfunction
-
CVB3 mutants, that arise with passage in polyamine-depleted conditions, contain mutations in the 2A protease (EC 3.4.22.29) and 3C protease (EC 3.4.22.28). These mutant proteases confer resistance to polyamine depletion. The 2A and 3C protease mutations also enhance reporter protease activity in polyamine-depleted conditions. The mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells
malfunction
infection of 2A protease activity-inactivated recombinant EV71 (EV71-2AC110S) failed to induce atypical stress granule (aSG) formation and only induced typical stress granule (tSG) formation, which is PKR and eIF2alpha phosphorylation-dependent. When the protease activity of 2A in EV71 is blocked (EV71-2AC110S), the tSGs but not aSGs appear in infected cells
malfunction
-
overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5
malfunction
-
viral 2Apro proteolytic activity is key process by disrupting the ERK signaling cascade. Disruption of the ERK signaling cascade interrupts viral 2Aprocatalysed processing of eIF4GI, overview. Inhibition of the ERK signaling cascade decreases 2Apro-mediated vIRES-dependent translation in other enteroviruses
malfunction
-
CVB3 mutants, that arise with passage in polyamine-depleted conditions, contain mutations in the 2A protease (EC 3.4.22.29) and 3C protease (EC 3.4.22.28). These mutant proteases confer resistance to polyamine depletion. The 2A and 3C protease mutations also enhance reporter protease activity in polyamine-depleted conditions. The mutations promote cleavage of cellular eIF4G during infection of polyamine-depleted cells
-
malfunction
Enterovirus A71 BrCR
-
infection of 2A protease activity-inactivated recombinant EV71 (EV71-2AC110S) failed to induce atypical stress granule (aSG) formation and only induced typical stress granule (tSG) formation, which is PKR and eIF2alpha phosphorylation-dependent. When the protease activity of 2A in EV71 is blocked (EV71-2AC110S), the tSGs but not aSGs appear in infected cells
-
physiological function
-
cleavage of eIF4G by PV 2Apro in mammalian cells modifies the requirement for eIF2 in translation directed by picornavirus IRESs. Cleavage of eIF4G by PV 2Apro establishes a mechanism for IRES-driven translation that is cap- and eIF2 independent
physiological function
-
Poliovirus 2A protease is able to confer high translatability on picornavirus IRESs when these are transcribed from sindbis virus replicons
physiological function
2A protease is the key viral component that triggers stress granule formation
physiological function
2A protease is the key viral component that triggers stress granule formation
physiological function
-
cleavage of serum response factor mediated by enteroviral protease 2A contributes to impaired cardiac function in mice
physiological function
-
expression of 2A protease induces a selective nucleo-cytoplasm translocation of several important RNA binding proteins and splicing factors. The enzyme can target alternative pre-mRNA splicing by regulating protein shuttling between the nucleus and the cytoplasm. The enzyme regulates alternative splicing of the Fas exon 6
physiological function
-
the enzyme binds to and stabilizes mouse double minute 4, thus in turn, it enhances the mitochondrial localization of p53 and promotes apoptosis in glioma cells
physiological function
-
death-associated protein 5 (DAP5) is cleaved during CVB3 infection by coxsackievirus B3 2A protease. Viral protease 2A but not 3C (EC 3.4.22.28) is responsible for DAP5 cleavage generating 45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments, respectively. Cleavage of DAP5 facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes. Also eukaryotic translation initiation factor 4G (eIF4G) is cleaved during infection by the enterovirus protease leading to the shutoff of cellular cap-dependent translation, but it does not affect the initiation of cap-independent translation of mRNAs containing an internal ribosome entry site (IRES). DAP5 is cleaved at amino acid G434. Upon cleavage, DAP5-N largely translocates to the nucleus at the later time points of infection, whereas the DAP5-C largely remains in the cytoplasm. DAP5-N expression promotes CVB3 replication and progeny release. On the other hand, DAP5-C exerts a dominant-negative effect on cap-dependent translation. DAP5 is cleaved into N- and C-terminal-truncated forms during CVB3 infection in vitro and in vivo and is transcriptionally downregulated. DAP5-N and DAP5-C differentially regulate translation of p53 and Bcl-2 and result in apoptotic cell death. DAP5-N and DAP5-C differentially alter translation but not transcription of IRES-containing genes p53 and Bcl-2
physiological function
-
enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein
physiological function
-
enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein
physiological function
-
enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enterovirus 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. 2Apro is a major enteroviral security protein
physiological function
-
enterovirus 2Apro plays a key role in inhibiting innate antiviral cellular responses. The direct cleavage of eIF4G by 2Apro contributes to the suppression of stress granule (SG) formation. Cleavage of eIF4G impairs the recruitment of 40S ribosomes to mRNAs, thereby altering the composition of mRNPs, which, in turn, may affect their recruitment to SGs. The observation that 2Apro triggers SG formation by cleavage of eIF4G. During enterovirus infection, several signaling molecules in the RLR pathway have been suggested to be cleaved by 2Apro and 3Cpro (EC 3.4.22.28). Enzyme 2Apro is the viral protease responsible for cleaving MAVS. Addition of recombinant 2Apro, but not 3Cpro, to cell lysates results in the appearance of MAVS cleavage products of the same size as those observed in infected cells. These cleavage products are also observed when 2Apro, but not 3Cpro, is expressed by a recombinant encephalomyocarditis virus (EMCV), a picornavirus that by itself does not cleave components of the RLR pathway. Enterovirus 2Apro, but not 3Cpro, suppresses the induction of IFN-alpha/beta gene transcription in HeLa cells. Heterologous expression of 2Apro during EMCV infection (EMCV-2Apro) nearly completely blocks IFN-beta gene transcription (about 500fold reduction) indicates that it is unlikely that suppression of SG formation by 2Apro is the major contributing factor in the viral suppression of IFN-beta gene transcription. 2Apro is a major enteroviral security protein
physiological function
-
Grb2-associated binding protein 2 (GAB2) is cleaved at G238 during CV-B3 infection by viral proteinase 2A. Knockdown of GAB2 significantly inhibits the synthesis of viral protein and subsequent viral progeny production, accompanied by reduced levels of phosphorylated p38, suggesting a pro-viral function for GAB2 linked to p38 activation. Expression of the cleavage products of GAB2 does not further enhance viral replication, indicating that GAB2 cleavage results in its loss-of-function, rather than gain-of-function in supporting viral replication that represents a distinct host defense mechanism
physiological function
poliovirus 2Apro plays a leading role in autocatalytic cleavage process of poliovirus polyprotein. 2Apro is involved in cleavage of eukaryotic translation initiation factor 4G (eIF4G)
physiological function
-
the 2A and 3C picornaviral proteases function to cleave both host and viral proteins. 3C protease is responsible for the majority of viral polyprotein cleavage, while 2A facilitates the cleavage between the P1 and P2 protein segments. Polyamines are crucial to protease function during picornavirus infection
physiological function
the 2A protease (2Apro) of human rhinoviruses (HRVs) plays important roles in the propagation of the virus and the modulation of host signal pathways to facilitate viral replication. The 2A protease (2Apro) specifically cleaves homologues of the human eukaryotic initiation factors eIF4GI and eIF4GII, which are required for cap-dependent mRNA translation by the ribosome. EIF4G is part of the initiation-factor complex eIF4F, which comprises the unwinding protease eIF4A and the cap-binding protein eIF4E. The complex recruits capped cellular mRNA to the ribosome for translation. Cleavage of eIF4G by HRV 2Apro impairs this process and shuts down cap-dependent translation of mRNA. Since the initiation of protein synthesis by picornaviruses is not cap-dependent, but requires the internal ribosome-entry site (IRES) present in the 5'-UTR of the picornavirus mRNA, shutting down the host cap-dependent translation machinery does not affect the synthesis of picornavirus proteins
physiological function
the 2A protease of enterovrius 71 (EV71) induces atypical stress granule (aSG), but not typical stress granule (tSG) formation, via cleavage of eIF4GI. Furthermore, 2A is required and sufficient to inhibit tSGs formation induced by EV71 infection, sodium arsenite, or heat shock. EV71-induced aSGs are beneficial to viral translation through sequestering only cellular mRNAs, but not viral mRNAs. Thus, EV71 infection induces tSG formation via the PKR-eIF2alpha pathway, and on the other hand, 2A, but not 3C protease (EC 3.4.22.28), blocks tSG formation
physiological function
-
the enzymatic activity of virally encoded 2Apro is essential to the stimulation of vIRES mediated translation. Key role of ERK cascade in maintaining 2Apro proteolytic activity required to maximize EV IRES activity at different stages of viral lifecycle
physiological function
-
the enzyme cleaves cellular transcription factor nuclear factor of activated T cells 5/tonicity enhancer binding protein (NFAT5/TonEBP). The 70-kDa N-terminal cleavage product (p70-NFAT5, amino acid residues 175-471 within the N-terminal fragment of NFAT5) exerts a dominant negative effect on the full-length NFAT5 protein. Elevated expression of NFAT5 to counteract viral protease cleavage, especially overexpression of a non-cleavable mutant of NFAT5, significantly inhibits CVB3 replication. Ectopic expression of NFAT5 results in elevated expression of inducible nitric oxide synthase (iNOS), a factor reported to inhibit CVB3 replication. The anti-CVB3 activity of NFAT5 is impaired during CVB3 infection due to 2A-mediated cleavage of NFAT5
physiological function
-
the human rhinovirus (HRV) 3C (EC 3.4.22.28) and 2A proteases (3Cpro and 2Apro, respectively) are critical in HRV infection, as they are required for viral polyprotein processing as well as proteolysing key host factors to facilitate virus replication. 2Apro activity is required to allow 3Cpro precursor 3CD (HRV 3CD) access to the nucleus. The activity of both 2Apro and 3Cpro is required for 3CD entry into the nucleus. Temporal activities of 2Apro and 3CD/3Cpro activities in HRV serotype16 infection
physiological function
-
the 2A and 3C picornaviral proteases function to cleave both host and viral proteins. 3C protease is responsible for the majority of viral polyprotein cleavage, while 2A facilitates the cleavage between the P1 and P2 protein segments. Polyamines are crucial to protease function during picornavirus infection
-
physiological function
Enterovirus A71 BrCR
-
the 2A protease of enterovrius 71 (EV71) induces atypical stress granule (aSG), but not typical stress granule (tSG) formation, via cleavage of eIF4GI. Furthermore, 2A is required and sufficient to inhibit tSGs formation induced by EV71 infection, sodium arsenite, or heat shock. EV71-induced aSGs are beneficial to viral translation through sequestering only cellular mRNAs, but not viral mRNAs. Thus, EV71 infection induces tSG formation via the PKR-eIF2alpha pathway, and on the other hand, 2A, but not 3C protease (EC 3.4.22.28), blocks tSG formation
-
physiological function
-
2A protease is the key viral component that triggers stress granule formation
-
additional information
structure-function analysis of poliovirus 2A protease, three-dimensional structure homology modelling using the crystal structure of coxsakievirus B4 as a template. Protein structure and protein-ligand-drug binding site predictions. Mutation pattern, intrinsic disorder regions (IDRs), hydrophobic regions, drug binding sites (DBS) and subcellular localization are identified, overview
additional information
structure-function analysis of poliovirus 2A protease, three-dimensional structure homology modelling using the crystal structure of coxsakievirus B4 as a template. Protein structure and protein-ligand-drug binding site predictions. Mutation pattern, intrinsic disorder regions (IDRs), hydrophobic regions, drug binding sites (DBS) and subcellular localization are identified, overview
additional information
the 2A proteases of other picornaviruses such as poliovirus and coxsackievirus also induce aSG formation and blocked tSG formation
additional information
-
the 2A proteases of other picornaviruses such as poliovirus and coxsackievirus also induce aSG formation and blocked tSG formation
additional information
the enzyme structure contains a conserved His-Asp-Cys catalytic triad and a Zn2+-binding site. Comparison with other 2Apro structures from enteroviruses reveals that the substrate-binding cleft of 2Apro from HRV-C15 exhibits a more open conformation, which presumably favours substrate binding, structure comparisons, overview
additional information
-
the enzyme structure contains a conserved His-Asp-Cys catalytic triad and a Zn2+-binding site. Comparison with other 2Apro structures from enteroviruses reveals that the substrate-binding cleft of 2Apro from HRV-C15 exhibits a more open conformation, which presumably favours substrate binding, structure comparisons, overview
additional information
Enterovirus A71 BrCR
-
the 2A proteases of other picornaviruses such as poliovirus and coxsackievirus also induce aSG formation and blocked tSG formation
-
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D136N
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
D39E
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
G122E
the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
L40F
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
S67F
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
V120M
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y89L
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y90L
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
D136N
-
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
-
D39E
-
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
-
G122E
-
the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
-
L40F
-
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
-
S67F
-
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
-
C110S
construction of catalytically inactive enzyme mutant EV71-2AC110S
D136N
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
D144A
the mutant shows increased activity compared to the wild type enzyme
D39E
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
E145A
the mutant shows strongly reduced activity compared to the wild type enzyme
G122E
the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
H21N/D39E/C110A
-
site-directed mutagenesis, a EV-A71 2Apro deleted replicon plasmid is constructed by deletion mutagenesis of the wild-type EV-A71 replicon by mutation at three positions (mutations of H21N, D39E, and C110A) of the 2Apro coding sequence
L40F
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
R55A
the mutant shows reduced activity compared to the wild type enzyme
S67F
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
V120M
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y89L
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y90L
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
C110S
Enterovirus A71 BrCR
-
construction of catalytically inactive enzyme mutant EV71-2AC110S
-
G60R
-
mutant is devoid of eIF4G cleavage activity
134Rstop
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
C101S
-
intramolecular cleavage is reduced to 52% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 20% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme
C106S
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
C112S
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C138A
-
intramolecular cleavage is reduced to 90% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 200% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme
C52A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C54A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C61A
-
intramolecular cleavage is reduced to 54% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 40% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
D105N
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
D105T
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
D132R/R134D
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
D132T
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
D35A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
D35E
-
intramolecular cleavage is reduced to 16% of the wild-type activity, cleavage of P8-P8' is completely abolished
D35T
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
DELTAG104
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
DELTAG107/108
-
cleavage of P8-P8' is completely abolished
F130L
-
intramolecular cleavage is completely abolished
F130S
-
intramolecular cleavage is completely abolished
F130V
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
F136V
-
intramolecular cleavage is reduced to 57% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 25% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
G115A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
G115S
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
G118A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
G118S
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
G123A
-
intramolecular cleavage is reduced to 23% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is less than 10% of that of the wild-type enzyme
G123A/G124A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
G123S
-
intramolecular cleavage is reduced to 20% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is below 10% of that of the wild-type enzyme
G124A
-
intramolecular cleavage is reduced to 22% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 9% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
G124S
-
intramolecular cleavage is reduced to 30% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
H114G
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
H135stop
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
H18A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
H18Y
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
K113P/H114A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
N16A
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
R134Q
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished, no cleavage of eIF4G is detected
T121Y
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
Y289R
-
inactive, substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y289R/A104C
-
substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y289R/A104S
-
substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y85K
-
intramolecular cleavage is reduced to 82% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 39% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y86F
-
intramolecular cleavage is reduced to 62% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 21% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y86K
-
intramolecular cleavage is reduced to 71% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 34% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
V54A
-
a BseRI fragment 4742-6148 is transferred from Se1-3C-02 DNA to pT7M, leads to defects in trans but not cis cleavage
Y88L
-
the BstEII fragment of picornavirus DNA from nucleotide 3240-3930 is replaced with a PCR product containing the appropriate mutation, the growth of picornavirus mutant is similar to that of wild-type virus in untreated cells but is completely inhibited in IFN-alpha-treated cells
Y88S
-
the BstEII fragment of picornavirus DNA from nucleotide 3240-3930 is replaced with a PCR product containing the appropriate mutation, the growth of picornavirus mutant is similar to that of wild-type virus in untreated cells but is completely inhibited in IFN-alpha-treated cells
R20D
-
significant defect in self-cleavage activity
R20G
-
significant defect in self-cleavage activity
R20P
-
complete inactivation, no self-cleavage activity
R20V
-
significant defect in self-cleavage activity
H114N
-
mutant enzyme does not contain Zn2+
H114N
-
intramolecular cleavage and cleavage of P8-P8' is completely abolished
L19S
-
cleavage of P8-P8' is reduced to 42% of the wild-type activity
L19S
-
intramolecular cleavage activity is reduced to 80% of that of the wild-type activity, cleavage of P8-P8' is reduced to 42% of the wild-type activity
Y85T
-
intramolecular cleavage is reduced to 74% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 32% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y85T
-
intramolecular cleavage is reduced to 27% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
additional information
-
generation of inactive mutant 2A29K through site-directed mutagenesis
additional information
-
overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5
additional information
-
generation of inactive mutant 2A29K through site-directed mutagenesis
-
additional information
-
stable expression of enzyme in HeLa cell lines. Expression of enzyme leads to apoptosis, indicated by nuclear fragmentation, DNA breakdown and phosphatidylserine translocation. Enzyme induces the cleavage of poly-ADP-ribose-polymerase, which is blocked by the caspase-3 inhibitor peptide Asp-Glu-Val-Asp
additional information
-
recombinant protein with His-tag, no enzymic activity upon eukaryotic initiation factor 4G I
additional information
-
the presence of an extensive C-terminal helix, in which Asp132, Arg134, Phe130 and Phe136 play important roles, explains why mutations in this region are generally detrimental to proteinase activity.The zinc-binding motif comprises Cys52, Cys54, Cys112 and His114. Exchange of these residues inactivates the enzyme
additional information
-
modification of R20 to every amino acid possible
additional information
-
substitution mutants of position R20 produce less severe disease
additional information
-
substitution mutants of position R20 produce less severe disease
-
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Krusslich, H.G.; Wimmer, E.
Viral proteinases
Annu. Rev. Biochem.
57
701-754
1988
coxsackievirus, enterovirus, Hepatovirus A, Human rhinovirus sp., picornaviridae, Enterovirus C
brenda
Glaser, W.; Skern, T.
Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro
FEBS Lett.
480
151-155
2000
Human rhinovirus sp.
brenda
Bazan, J.F.; Fletterick, R.J.
Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications
Proc. Natl. Acad. Sci. USA
85
7872-7876
1988
coxsackievirus, enterovirus, Human rhinovirus sp., picornaviridae, Enterovirus C
brenda
Skern, T.; Liebig, H.D.
Picornains 2A and 3C
Methods Enzymol.
244
583-595
1994
coxsackievirus, enterovirus, Human rhinovirus sp., picornaviridae, Enterovirus C
brenda
Toyoda, H.; Nicklin, M.J.H.; Murray, M.G.; Anderson, C.W.; Dunn, J.J.; Studier, F.W.; Wimmer, E.
A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
Cell
45
761-770
1986
Enterovirus C
brenda
Knig, H.; Rosenwirth, B.
Purification and partial characterization of poliovirus protease 2A by means of a functional assay
J. Virol.
62
1243-1250
1988
Enterovirus C
brenda
Alvey, J.C.; Wyckoff, E.E.; Yu, S.F.; Lloyd, R.; Ehrenfeld, E.
cis- and trans-cleavage activities of poliovirus 2A protease expressed in Escherichia coli
J. Virol.
65
6077-6083
1991
Enterovirus C
brenda
Yu, S.F.; Lloyd, R.
Characterization of the roles of conserved cysteine and histidine residues in poliovirus 2A protease
Virology
186
725-735
1992
coxsackievirus, enterovirus, Human rhinovirus sp., Enterovirus C
brenda
Sommergruber, W.; Ahorn, H.; Zphel, A.; Maurer-Fogy, I.; Fessl, F.; Schnorrenberg, G.; Liebig, H.D.; Blaas, D.; Kuechler, E.; Skern, T.
Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A
J. Biol. Chem.
267
22639-22644
1992
Human rhinovirus sp.
brenda
Liebig, H.D.; Ziegler, E.; Yan, R.; Hartmut, K.; Klump, H.; Kowalski, H.; Blaas, D.; Sommergruber, W.; Frasel, L.; Lamphear, B.; Rhoads, R.; Kuechler, E.; Skern, T.
Purification of two picornaviral 2A proteinases: interaction with eIF-4 gamma and influence on in vitro translation
Biochemistry
32
7581-7588
1993
coxsackievirus, Human rhinovirus sp.
brenda
Lamphear, B.J.; Yan, R.; Yang, F.; Waters, D.; Liebig, H.D.; Klump, H.; Kuechler, E.; Skern, T.; Rhoads, R.E.
Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus
J. Biol. Chem.
268
19200-19203
1993
coxsackievirus, Human rhinovirus sp.
brenda
Sommergruber, W.; Casari, G.; Fessl, F.; Seipelt, J.; Skern, T.
The 2A proteinase of human rhinovirus is a zinc containing enzyme
Virology
204
815-818
1994
Human rhinovirus sp.
brenda
Sommergruber, W.; Ahorn, H.; Klump, H.; Seipelt, J.; Zphel, A.; Fessl, F.; Krystek, E.; Blaas, D.; Kuechler, E.; Liebig, H.D.; Skern, T.
2A Proteinases of coxsackie- and rhinovirus cleave peptides derived from eIF-4 gamma via a common recognition motif
Virology
198
741-745
1994
coxsackievirus, Human rhinovirus sp.
brenda
Voss, T.; Meyer, R.; Sommergruber, W.
Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity
Protein Sci.
4
2526-2531
1995
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Human poliovirus 1 (T1WTS3), Human poliovirus 1 (T1WU96)
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Coxsackievirus B3, Coxsackievirus B3 Nancy
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